4neq: Difference between revisions
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==The structure of UDP-GlcNAc 2-epimerase from Methanocaldococcus jannaschii== | ==The structure of UDP-GlcNAc 2-epimerase from Methanocaldococcus jannaschii== | ||
<StructureSection load='4neq' size='340' side='right' caption='[[4neq]], [[Resolution|resolution]] 2.85Å' scene=''> | <StructureSection load='4neq' size='340' side='right' caption='[[4neq]], [[Resolution|resolution]] 2.85Å' scene=''> | ||
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">wecB, MJ1504 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243232 METJA])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">wecB, MJ1504 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243232 METJA])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/UDP-N-acetylglucosamine_2-epimerase_(non-hydrolyzing) UDP-N-acetylglucosamine 2-epimerase (non-hydrolyzing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.1.3.14 5.1.3.14] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/UDP-N-acetylglucosamine_2-epimerase_(non-hydrolyzing) UDP-N-acetylglucosamine 2-epimerase (non-hydrolyzing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.1.3.14 5.1.3.14] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4neq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4neq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4neq RCSB], [http://www.ebi.ac.uk/pdbsum/4neq PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4neq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4neq OCA], [http://pdbe.org/4neq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4neq RCSB], [http://www.ebi.ac.uk/pdbsum/4neq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4neq ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4neq" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 20:07, 22 March 2017
The structure of UDP-GlcNAc 2-epimerase from Methanocaldococcus jannaschiiThe structure of UDP-GlcNAc 2-epimerase from Methanocaldococcus jannaschii
Structural highlights
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). Publication Abstract from PubMedUridine diphosphate N-acetylglucosamine (UDP-GlcNAc) 2-epimerase catalyzes the interconversion of UDP-GlcNAc to UDP-N-acetylmannosamine (UDP-ManNAc), which is used in the biosynthesis of cell surface polysaccharides in bacteria. Biochemical experiments have demonstrated that mutation of this enzyme causes changes in cell morphology and the thermoresistance of the cell wall. Here, we present the crystal structures of Methanocaldococcus jannaschii UDP-GlcNAc 2-epimerase in open and closed conformations. A comparison of these crystal structures shows that upon UDP and UDP-GlcNAc binding, the enzyme undergoes conformational changes involving a rigid-body movement of the C-terminal domain. We also present the crystal structure of Bacillus subtilis UDP-GlcNAc 2-epimerase in the closed conformation in the presence of UDP and UDP-GlcNAc. Although a structural overlay of these two closed-form structures reveals that the substrate-binding site is evolutionarily conserved, some areas of the allosteric site are distinct between the archaeal and bacterial UDP-GlcNAc 2-epimerases. This is the first report on the crystal structure of archaeal UDP-GlcNAc 2-epimerase, and our results clearly demonstrate the changes between the open and closed conformations of this enzyme. Proteins 2014. (c) 2014 Wiley Periodicals, Inc. Crystal structures of the archaeal UDP-GlcNAc 2-epimerase from Methanocaldococcus jannaschii reveal a conformational change induced by UDP-GlcNAc.,Chen SC, Huang CH, Shin Yang C, Liu JS, Kuan SM, Chen Y Proteins. 2014 Jan 27. doi: 10.1002/prot.24516. PMID:24470206[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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