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| | <StructureSection load='4tsd' size='340' side='right'caption='[[4tsd]], [[Resolution|resolution]] 1.53Å' scene=''> | | <StructureSection load='4tsd' size='340' side='right'caption='[[4tsd]], [[Resolution|resolution]] 1.53Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4tsd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Campylobacter_pylori Campylobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TSD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TSD FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4tsd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori_26695 Helicobacter pylori 26695]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TSD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4TSD FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.53Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4tsz|4tsz]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">C694_05325, HP_1029 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=85962 Campylobacter pylori])</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=4tsd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tsd OCA], [https://pdbe.org/4tsd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4tsd RCSB], [https://www.ebi.ac.uk/pdbsum/4tsd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4tsd ProSAT]</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=4tsd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tsd OCA], [http://pdbe.org/4tsd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4tsd RCSB], [http://www.ebi.ac.uk/pdbsum/4tsd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4tsd ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/O25673_HELPY O25673_HELPY] |
| | <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: Campylobacter pylori]] | + | [[Category: Helicobacter pylori 26695]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Percudani, R]] | + | [[Category: Percudani R]] |
| - | [[Category: Vallese, F]] | + | [[Category: Vallese F]] |
| - | [[Category: Zanotti, G]] | + | [[Category: Zanotti G]] |
| - | [[Category: Pfam family pf04074]]
| + | |
| - | [[Category: Unknown function]]
| + | |
| - | [[Category: Zinc binding]]
| + | |
| Structural highlights
Function
O25673_HELPY
Publication Abstract from PubMed
The proteins of the YhcH/YjgK/YiaL (DUF386) family have been implicated in the bacterial metabolism of host-derived sialic acids and biofilm formation, although their precise biochemical function remains enigmatic. We present here the crystal structure of protein HP1029 from Helicobacter pylori. The protein is a homodimer, in which each monomer comprises a molecular core formed by 12 antiparallel beta-strands arranged in two beta-sheets flanked by helices. The sandwich formed by the sheets assumes the shape of a funnel opened at one end, with a zinc ion present at the bottom of the funnel. The crystal structure unequivocally shows that HP1029 belongs to the DUF386 family. Although no bioinformatics evidence has been found for sialic acid catabolism in H. pylori, the genomic context of HP1029 in Helicobacter and related organisms suggests a possible role in the metabolism of bacterial surface saccharides, such as pseudaminic acid and its derivatives.
The crystal structure of Helicobacter pylori HP1029 highlights the functional diversity of the sialic acid-related DUF386 family.,Vallese F, Percudani R, Fischer W, Zanotti G FEBS J. 2015 Jun 12. doi: 10.1111/febs.13344. PMID:26096900[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Vallese F, Percudani R, Fischer W, Zanotti G. The crystal structure of Helicobacter pylori HP1029 highlights the functional diversity of the sialic acid-related DUF386 family. FEBS J. 2015 Jun 12. doi: 10.1111/febs.13344. PMID:26096900 doi:http://dx.doi.org/10.1111/febs.13344
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