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| | ==Crystal structure of UDP-GlcNAc 2-epimerase NeuC complexed with UDP== | | ==Crystal structure of UDP-GlcNAc 2-epimerase NeuC complexed with UDP== |
| - | <StructureSection load='5zlt' size='340' side='right' caption='[[5zlt]], [[Resolution|resolution]] 2.50Å' scene=''> | + | <StructureSection load='5zlt' size='340' side='right'caption='[[5zlt]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5zlt]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZLT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZLT FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5zlt]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Acinetobacter_baumannii Acinetobacter baumannii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZLT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZLT FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</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,N'-diacetylbacillosamine_2-epimerase_(hydrolyzing) UDP-N,N'-diacetylbacillosamine 2-epimerase (hydrolyzing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.184 3.2.1.184] </span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></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=5zlt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zlt OCA], [http://pdbe.org/5zlt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zlt RCSB], [http://www.ebi.ac.uk/pdbsum/5zlt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zlt ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5zlt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zlt OCA], [https://pdbe.org/5zlt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zlt RCSB], [https://www.ebi.ac.uk/pdbsum/5zlt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zlt ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A154EJU5_ACIBA A0A154EJU5_ACIBA] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Chen, Y]] | + | [[Category: Acinetobacter baumannii]] |
| - | [[Category: Hsieh, T J]] | + | [[Category: Large Structures]] |
| - | [[Category: Ko, T P]] | + | [[Category: Chen Y]] |
| - | [[Category: Yang, C S]] | + | [[Category: Hsieh TJ]] |
| - | [[Category: Hydrolase]] | + | [[Category: Ko TP]] |
| - | [[Category: Neuc]] | + | [[Category: Yang CS]] |
| - | [[Category: Udp n-acetylglucosamine 2-epimerase]]
| + | |
| Structural highlights
Function
A0A154EJU5_ACIBA
Publication Abstract from PubMed
Sialic acid presentation on the cell surface by some pathogenic strains of bacteria allows their escape from the host immune system. It is one of the major virulence factors. Bacterial biosynthesis of sialic acids starts with the conversion of UDP-GlcNAc to UDP and ManNAc by a hydrolyzing 2-epimerase. Here we present the crystal structure of this enzyme, named NeuC, from Acinetobacter baumannii The protein folds into two Rossmann-like domains and forms dimers and tetramers as does the epimerase part of the bifunctional UDP-GlcNAc 2-epimerase / ManNAc kinase (GNE). In contrast to human GNE, which showed only the closed conformation, the NeuC crystals contained both open and closed protomers in each dimer. Substrate soaking changed the space group from C2221 to P212121 In addition to UDP, an intermediate-like ligand was seen bound to the closed protomer. The UDP-binding mode in NeuC was similar to that in GNE, although a few side chains were rotated away. NeuC lacks the CMP-Neu5Ac binding site for allosteric inhibition of GNE. However, the two enzymes as well as other NeuC homologues (but not SiaA from Neisseria meningitidis) appear to be common in tetrameric organization. The revised two-base catalytic mechanism may involve His125 (Glu134 in GNE), as suggested by mutant activity analysis.
The tetrameric structure of sialic-acid-synthesizing UDP-GlcNAc 2-epimerase from Acinetobacter baumannii: a comparative study with human GNE.,Ko TP, Lai SJ, Hsieh TJ, Yang CS, Chen Y J Biol Chem. 2018 May 15. pii: RA118.001971. doi: 10.1074/jbc.RA118.001971. PMID:29764940[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ko TP, Lai SJ, Hsieh TJ, Yang CS, Chen Y. The tetrameric structure of sialic-acid-synthesizing UDP-GlcNAc 2-epimerase from Acinetobacter baumannii: a comparative study with human GNE. J Biol Chem. 2018 May 15. pii: RA118.001971. doi: 10.1074/jbc.RA118.001971. PMID:29764940 doi:http://dx.doi.org/10.1074/jbc.RA118.001971
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