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4nes

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'''Unreleased structure'''
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{{STRUCTURE_4nes| PDB=4nes | SCENE= }}
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===Crystal structure of Methanocaldococcus jannaschii UDP-GlcNAc 2-epimerase in complex with UDP-GlcNAc and UDP===
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{{ABSTRACT_PUBMED_24470206}}
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The entry 4nes is ON HOLD until Paper Publication
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==Function==
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[[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).
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Authors: Chen, S.C., Yang, C.S., Huang, C.H., Chen, Y.
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==About this Structure==
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[[4nes]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NES OCA].
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Description: Crystal structure of Methanocaldococcus jannaschii UDP-GlcNAc 2-epimerase in complex with UDP-GlcNAc and UDP
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==Reference==
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<ref group="xtra">PMID:024470206</ref><references group="xtra"/><references/>
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[[Category: Chen, S C.]]
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[[Category: Chen, Y.]]
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[[Category: Huang, C H.]]
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[[Category: Yang, C S.]]
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[[Category: Isomerase]]
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[[Category: Udp-glcnac 2-epimerase]]
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[[Category: Udp-glycosyltransferase/glycogen phosphorylase fold]]

Revision as of 07:46, 23 April 2014

Template:STRUCTURE 4nes

Contents

Crystal structure of Methanocaldococcus jannaschii UDP-GlcNAc 2-epimerase in complex with UDP-GlcNAc and UDP

Template:ABSTRACT PUBMED 24470206

Function

[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 Structure

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

Reference

  • 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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