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You searched for: Author "Isupov, Michail N." Remove constraint Author: "Isupov, Michail N." Subject crystal structure Remove constraint Subject: crystal structure
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1. Structural Evidence for an Octameric Ring Arrangement of SARM1

Author:
Isupov, Michail N.,   et al.   ; Sporny, Michael; Guez-Haddad, Julia; Lebendiker, Mario; Ulisse, Valeria; Volf, Allison; Mim, Carsten; Opatowsky, Yarden;     Show all 8 Authors
Source:
Journal of molecular biology 2019 v.431 no.19 pp. 3591-3605
ISSN:
0022-2836
Subject:
adenosine diphosphate; animal injuries; apoptosis; brain; crystal structure; cultured cells; drug development; drugs; electron microscopy; electrostatic interactions; epitopes; hydrophobicity; mutation; oligomerization; protein subunits; proteins; ribose; spinal cord; therapeutics
Abstract:
... SARM1 induces axonal degeneration in response to various insults and is therefore considered an attractive drug target for the treatment of neuro-degenerative diseases as well as for brain and spinal cord injuries. SARM1 activity depends on the integrity of the protein's SAM domains, as well as on the enzymatic conversion of NAD+ to ADPR (ADP Ribose) products by the SARM1's TIR domain. Therefore, ...
DOI:
10.1016/j.jmb.2019.06.030

2. An N-Terminal Extension to UBA5 Adenylation Domain Boosts UFM1 Activation: Isoform-Specific Differences in Ubiquitin-like Protein Activation

Author:
Isupov, Michail N.,   et al.   ; Soudah, Nadine; Padala, Prasanth; Hassouna, Fouad; Kumar, Manoj; Mashahreh, Bayan; Lebedev, Andrey A.; Cohen-Kfir, Einav; Wiener, Reuven;     Show all 9 Authors
Source:
Journal of molecular biology 2019 v.431 no.3 pp. 463-478
ISSN:
0022-2836
Subject:
adenosine triphosphate; crystal structure; humans; proteins
Abstract:
... Modification of proteins by the ubiquitin-like protein, UFM1, requires activation of UFM1 by the E1-activating enzyme, UBA5. In humans, UBA5 possesses two isoforms, each comprising an adenylation domain, but only one containing an N-terminal extension. Currently, the role of the N-terminal extension in UFM1 activation is not clear. Here we provide structural and biochemical data on UBA5 N-terminal ...
DOI:
10.1016/j.jmb.2018.10.007

3. Structural Principles in Robo Activation and Auto-inhibition

Author:
Isupov, Michail N.,   et al.   ; Barak, Reut; Yom-Tov, Galit; Guez-Haddad, Julia; Gasri-Plotnitsky, Lital; Maimon, Roy; Cohen-Berkman, Moran; McCarthy, Andrew A.; Perlson, Eran; Henis-Korenblit, Sivan; Opatowsky, Yarden;     Show all 11 Authors
Source:
Cell 2019 v.177 no.2 pp. 272-285.e16
ISSN:
0092-8674
Subject:
brain; crystal structure; dimerization; humans; ligands; mice; models; neurons; receptors
Abstract:
... Proper brain function requires high-precision neuronal expansion and wiring, processes controlled by the transmembrane Roundabout (Robo) receptor family and their Slit ligands. Despite their great importance, the molecular mechanism by which Robos’ switch from “off” to “on” states remains unclear. Here, we report a 3.6 Å crystal structure of the intact human Robo2 ectodomain (domains D1–8). We dem ...
DOI:
10.1016/j.cell.2019.02.004

4. The crystal structure and conformations of an unbranched mixed tri-ubiquitin chain containing K48 and K63 linkages

Author:
Isupov, Michail N.,   et al.   ; Padala, Prasanth; Soudah, Nadine; Giladi, Moshe; Haitin, Yoni; Wiener, Reuven;     Show all 6 Authors
Source:
Journal of Molecular Biology 2017
ISSN:
0022-2836
Subject:
X-radiation; crystal structure; functional properties; lysine; ubiquitin
Abstract:
... The ability of ubiquitin to function in a wide range of cellular processes is ascribed to its capacity to cause a diverse spectrum of modifications. While a target protein can be modified with monoubiquitin, it can also be modified with ubiquitin chains. The latter include seven types of homotypic chains as well as mixed ubiquitin chains. In a mixed chain, not all the isopeptide bonds are restrict ...
DOI:
10.1016/j.jmb.2017.10.027

5. Structural studies of a thermophilic esterase from a new Planctomycetes species, Thermogutta terrifontis

Author:
Isupov, Michail N.,   et al.   ; Sayer, Christopher; Bonch‐Osmolovskaya, Elizaveta; Littlechild, Jennifer A.;     Show all 4 Authors
Source:
The FEBS journal 2015 v.282 no.15 pp. 2846-2857
ISSN:
1742-464X
Subject:
Escherichia coli; acetates; active sites; alcohols; amino acids; butyrates; catalytic activity; crystal structure; esterases; genetic databases; ligands; malates; mutants; propionic acid; thermophilic bacteria
Abstract:
... Thermogutta terrifontis esterase (TtEst), a carboxyl esterase identified in the novel thermophilic bacterium T. terrifontis from the phylum Planctomycetes, has been cloned and over‐expressed in Escherichia coli. The enzyme has been characterized biochemically and shown to have activity towards small p‐nitrophenyl (pNP) carboxylic esters, with optimal activity for pNP‐propionate. The enzyme retaine ...
DOI:
10.1111/febs.13326

6. Biochemical and structural characterisation of a haloalkane dehalogenase from a marine Rhodobacteraceae

Author:
Isupov, Michail N.,   et al.   ; Novak, Halina R.; Sayer, Christopher; Gotz, Dorothee; Spragg, Andrew Mearns; Littlechild, Jennifer A.;     Show all 6 Authors
Source:
FEBS letters 2014 v.588 pp. 1616-1622
ISSN:
0014-5793
Subject:
Escherichia coli; Rhodobacteraceae; active sites; carbon; crystal structure; hydrophobicity
Abstract:
... A putative haloalkane dehalogenase has been identified in a marine Rhodobacteraceae and subsequently cloned and over-expressed in Escherichia coli. The enzyme has highest activity towards the substrates 1,6-dichlorohexane, 1-bromooctane, 1,3-dibromopropane and 1-bromohexane. The crystal structures of the enzyme in the native and product bound forms reveal a large hydrophobic active site cavity. A ...
DOI:
10.1016/j.febslet.2014.02.056

7. Discovery and characterization of thermophilic limonene‐1,2‐epoxide hydrolases from hot spring metagenomic libraries

Author:
Isupov, Michail N.,   et al.   ; Ferrandi, Erica Elisa; Sayer, Christopher; Annovazzi, Celeste; Marchesi, Carlotta; Iacobone, Gianluca; Peng, Xu; Bonch‐Osmolovskaya, Elizaveta; Wohlgemuth, Roland; Littlechild, Jennifer A.; Monti, Daniela;     Show all 11 Authors
Source:
The FEBS journal 2015 v.282 no.15 pp. 2879-2894
ISSN:
1742-464X
Subject:
Rhodococcus erythropolis; crystal structure; drugs; epoxides; ethylene glycol; genetic databases; genomic libraries; hot springs; hydrolases; melting; metagenomics; mutagenesis; nucleotide sequences; polyethylene glycol; substrate specificity; temperature
Abstract:
... The epoxide hydrolases (EHs) represent an attractive option for the synthesis of chiral epoxides and 1,2‐diols which are valuable building blocks for the synthesis of several pharmaceutical compounds. A metagenomic approach has been used to identify two new members of the atypical EH limonene‐1,2‐epoxide hydrolase (LEH) family of enzymes. These two LEHs (Tomsk‐LEH and CH55‐LEH) show EH activities ...
DOI:
10.1111/febs.13328

8. Functional and structural characterisation of a viral cytochrome b5

Author:
Isupov, Michail N.,   et al.   ; Reid, Emma L.; Weynberg, Karen D.; Love, John; Littlechild, Jennifer A.; Wilson, William H.; Kelly, Steven L.; Lamb, David C.; Allen, Michael J.;     Show all 9 Authors
Source:
FEBS letters 2013 v.587 pp. 3633-3639
ISSN:
0014-5793
Subject:
crystal structure; cytochrome P-450; electron transfer; genes; horizontal gene transfer; humans; hydrophobicity; spectral analysis; transport proteins; viruses; yeasts
Abstract:
... Cytochrome b5 is a ubiquitous electron transport protein. The sequenced viral OtV-2 genome, which infects Ostreococcus tauri, was predicted to encode a putative cytochrome b5 enzyme. Using purified OtV-2 cytochrome b5 we confirm this protein has identical spectral properties to purified human cytochrome b5 and additionally that the viral enzyme can substitute for yeast cytochrome b5 in yeast cytoc ...
DOI:
10.1016/j.febslet.2013.09.035

9. The Fasciola hepatica thioredoxin: High resolution structure reveals two oxidation states

Author:
Isupov, Michail N.,   et al.   ; Line, Kirsty; Garcia-Rodriguez, Esther; Maggioli, Gabriela; Parra, Francisco; Littlechild, Jennifer A.;     Show all 6 Authors
Source:
Molecular and biochemical parasitology 2008 v.161 no.1 pp. 44-48
ISSN:
0166-6851
Subject:
Fasciola hepatica; active sites; crystal structure; cysteine; disulfide bonds; hosts; humans; oxidation; protein structure
Abstract:
... The Fasciola hepatica thioredoxin protein structure has been determined to 1.45Å resolution. This is the first example of a single crystal structure to show the active site cysteine residues in both the reduced and disulfide oxidised form. Consistent with this observation the process of oxidation appears to require very little rearrangement of the surrounding protein structure. The F. hepatica thi ...
DOI:
10.1016/j.molbiopara.2008.06.009

10. Crystal structure of D-serine dehydratase from Escherichia coli Proteins and proteomics

Author:
Isupov, Michail N.,   et al.   ; Urusova, Darya V.; Antonyuk, Svetlana; Kachalova, Galina S.; Obmolova, Galina; Vagin, Alexei A.; Lebedev, Andrey A.; Burenkov, Gleb P.; Dauter, Zbigniew; Bartunik, Hans D.; Lamzin, Victor S.; Melik-Adamyan, William R.; Mueller, Thomas D.; Schnackerz, Klaus D.;     Show all 14 Authors
Source:
Biochimica et biophysica acta 2012 v.1824 no.3 pp. 422-432
ISSN:
1878-1454
Subject:
Escherichia coli; active sites; ammonia; catalytic activity; crystal structure; data collection; hydrogen bonding; models; oxygen; pyridoxal; pyruvic acid; schiff bases; serine dehydratase
Abstract:
... D-Serine dehydratase from Escherichia coli is a member of the β-family (fold-type II) of the pyridoxal 5′-phosphate-dependent enzymes, catalyzing the conversion of D-serine to pyruvate and ammonia. The crystal structure of monomeric D-serine dehydratase has been solved to 1.97Å-resolution for an orthorhombic data set by molecular replacement. In addition, the structure was refined in a monoclinic ...
DOI:
10.1016/j.bbapap.2011.10.017

11. Papillomavirus E1 helicase assembly maintains an asymmetric state in the absence of DNA and nucleotide cofactors

Author:
Isupov, Michail N.,   et al.   ; Sanders, Cyril M.; Kovalevskiy, Oleg V.; Sizov, Dmytro; Lebedev, Andrey A.; Antson, Alfred A.;     Show all 6 Authors
Source:
Nucleic acids research 2007 v.35 no.19 pp. 6451-6457
ISSN:
0305-1048
Subject:
Papillomaviridae; mechanism of action; crystal structure; DNA; adenosine diphosphate; adenosine triphosphate; nucleic acid conformation; binding sites; hydrolysis; kinesin
Abstract:
... Concerted, stochastic and sequential mechanisms of action have been proposed for different hexameric AAA+ molecular motors. Here we report the crystal structure of the E1 helicase from bovine papillomavirus, where asymmetric assembly is for the first time observed in the absence of nucleotide cofactors and DNA. Surprisingly, the ATP-binding sites adopt specific conformations linked to positional c ...
DOI:
10.1093/nar/gkm705
PubMed:
17881379
PubMed Central:
PMC2095799