4neq: Difference between revisions

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'''Unreleased structure'''
{{STRUCTURE_4neq|  PDB=4neq  |  SCENE=  }}
===The structure of UDP-GlcNAc 2-epimerase from Methanocaldococcus jannaschii===
{{ABSTRACT_PUBMED_24470206}}


The entry 4neq is ON HOLD  until Paper Publication
==Function==
[[http://www.uniprot.org/uniprot/WECB_METJA WECB_METJA]] Catalyzes the reversible epimerization at C-2 of UDP-N-acetylglucosamine (UDP-GlcNAc) to produce UDP-N-acetylmannosamine (UDP-ManNAc), the activated donor of ManNAc residues (By similarity).


Authors: Chen, S.C., Yang, C.S., Huang, C.H., Chen, Y.
==About this Structure==
[[4neq]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NEQ OCA].  


Description: The structure of UDP-GlcNAc 2-epimerase from Methanocaldococcus jannaschii
==Reference==
<ref group="xtra">PMID:024470206</ref><references group="xtra"/><references/>
[[Category: Chen, S C.]]
[[Category: Chen, Y.]]
[[Category: Huang, C H.]]
[[Category: Yang, C S.]]
[[Category: Isomerase]]
[[Category: Udp-glcnac 2-epimerase]]
[[Category: Udp-glycosyltransferase/glycogen phosphorylase fold]]

Revision as of 10:42, 23 April 2014

Template:STRUCTURE 4neq

The structure of UDP-GlcNAc 2-epimerase from Methanocaldococcus jannaschiiThe structure of UDP-GlcNAc 2-epimerase from Methanocaldococcus jannaschii

Template:ABSTRACT PUBMED 24470206

FunctionFunction

[WECB_METJA] Catalyzes the reversible epimerization at C-2 of UDP-N-acetylglucosamine (UDP-GlcNAc) to produce UDP-N-acetylmannosamine (UDP-ManNAc), the activated donor of ManNAc residues (By similarity).

About this StructureAbout this Structure

4neq is a 1 chain structure. Full crystallographic information is available from OCA.

ReferenceReference

[xtra 1]

  1. Chen SC, Huang CH, Shin Yang C, Liu JS, Kuan SM, Chen Y. Crystal structures of the archaeal UDP-GlcNAc 2-epimerase from Methanocaldococcus jannaschii reveal a conformational change induced by UDP-GlcNAc. Proteins. 2014 Jan 27. doi: 10.1002/prot.24516. PMID:24470206 doi:http://dx.doi.org/10.1002/prot.24516

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