3hcg: Difference between revisions
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{{STRUCTURE_3hcg| PDB=3hcg | SCENE= }} | {{STRUCTURE_3hcg| PDB=3hcg | SCENE= }} | ||
===Structure of the C-terminal domain (MsrB) of Neisseria meningitidis PilB (reduced form)=== | ===Structure of the C-terminal domain (MsrB) of Neisseria meningitidis PilB (reduced form)=== | ||
{{ABSTRACT_PUBMED_19733575}} | |||
==Function== | |||
[[http://www.uniprot.org/uniprot/MSRAB_NEIMA MSRAB_NEIMA]] Has an important function as a repair enzyme for proteins that have been inactivated by oxidation (By similarity). Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. | |||
==About this Structure== | ==About this Structure== | ||
[[3hcg]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/ | [[3hcg]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Neimd Neimd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HCG OCA]. | ||
==Reference== | ==Reference== | ||
<ref group="xtra">PMID:019733575</ref>< | <ref group="xtra">PMID:019733575</ref><references group="xtra"/><references/> | ||
[[Category: | [[Category: Neimd]] | ||
[[Category: Favier, F.]] | [[Category: Favier, F.]] | ||
[[Category: Kauffmann, B.]] | [[Category: Kauffmann, B.]] | ||
Revision as of 04:22, 9 April 2014
Structure of the C-terminal domain (MsrB) of Neisseria meningitidis PilB (reduced form)
Template:ABSTRACT PUBMED 19733575
Function
[MSRAB_NEIMA] Has an important function as a repair enzyme for proteins that have been inactivated by oxidation (By similarity). Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
About this Structure
3hcg is a 4 chain structure with sequence from Neimd. Full crystallographic information is available from OCA.
Reference
- Ranaivoson FM, Neiers F, Kauffmann B, Boschi-Muller S, Branlant G, Favier F. Methionine sulfoxide reductase B displays a high level of flexibility. J Mol Biol. 2009 Nov 20;394(1):83-93. Epub 2009 Sep 4. PMID:19733575 doi:10.1016/j.jmb.2009.08.073
