1fvg
From Proteopedia
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|PDB= 1fvg |SIZE=350|CAPTION= <scene name='initialview01'>1fvg</scene>, resolution 1.6Å | |PDB= 1fvg |SIZE=350|CAPTION= <scene name='initialview01'>1fvg</scene>, resolution 1.6Å | ||
|SITE= | |SITE= | ||
- | |LIGAND= <scene name='pdbligand=DTT:2,3-DIHYDROXY-1,4-DITHIOBUTANE'>DTT</scene> | + | |LIGAND= <scene name='pdbligand=DTT:2,3-DIHYDROXY-1,4-DITHIOBUTANE'>DTT</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene> |
- | |ACTIVITY= [http://en.wikipedia.org/wiki/Peptide-methionine-(S)-S-oxide_reductase Peptide-methionine-(S)-S-oxide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.4.11 1.8.4.11] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptide-methionine-(S)-S-oxide_reductase Peptide-methionine-(S)-S-oxide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.4.11 1.8.4.11] </span> |
|GENE= | |GENE= | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY=[[1fva|1FVA]] | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fvg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fvg OCA], [http://www.ebi.ac.uk/pdbsum/1fvg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fvg RCSB]</span> | ||
}} | }} | ||
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[[Category: Matthews, B W.]] | [[Category: Matthews, B W.]] | ||
[[Category: Weissbach, H.]] | [[Category: Weissbach, H.]] | ||
- | [[Category: DTT]] | ||
[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:31:01 2008'' |
Revision as of 17:31, 30 March 2008
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, resolution 1.6Å | |||||||
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Ligands: | , | ||||||
Activity: | Peptide-methionine-(S)-S-oxide reductase, with EC number 1.8.4.11 | ||||||
Related: | 1FVA
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Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
CRYSTAL STRUCTURE OF BOVINE PEPTIDE METHIONINE SULFOXIDE REDUCTASE
Overview
Peptide methionine sulfoxide reductase (MsrA) reverses oxidative damage to both free methionine and methionine within proteins. As such, it helps protect the host organism against stochastic damage that can contribute to cell death. The structure of bovine MsrA has been determined in two different modifications, both of which provide different insights into the biology of the protein. There are three cysteine residues located in the vicinity of the active site. Conformational changes in a glycine-rich C-terminal tail appear to allow all three thiols to come together and to participate in catalysis. The structures support a unique, thiol-disulfide exchange mechanism that relies upon an essential cysteine as a nucleophile and additional conserved residues that interact with the oxygen atom of the sulfoxide moiety.
About this Structure
1FVG is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
Structure and mechanism of peptide methionine sulfoxide reductase, an "anti-oxidation" enzyme., Lowther WT, Brot N, Weissbach H, Matthews BW, Biochemistry. 2000 Nov 7;39(44):13307-12. PMID:11063566
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