3qbu

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<StructureSection load='3qbu' size='340' side='right'caption='[[3qbu]], [[Resolution|resolution]] 2.57&Aring;' scene=''>
<StructureSection load='3qbu' size='340' side='right'caption='[[3qbu]], [[Resolution|resolution]] 2.57&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3qbu]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Helpg Helpg]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QBU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QBU FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3qbu]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori_G27 Helicobacter pylori G27]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QBU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QBU FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5701&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3cl8|3cl8]], [[1z7a|1z7a]], [[2c1g|2c1g]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hp0310, HPG27_289 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=563041 HELPG])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3qbu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qbu OCA], [https://pdbe.org/3qbu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qbu RCSB], [https://www.ebi.ac.uk/pdbsum/3qbu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qbu 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=3qbu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qbu OCA], [https://pdbe.org/3qbu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qbu RCSB], [https://www.ebi.ac.uk/pdbsum/3qbu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qbu ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/PGDAE_HELPG PGDAE_HELPG] Catalyzes the N-deacetylation of peptidoglycan (PG), an important mechanism that appears to confer lysozyme resistance and to mitigate host immune detection; this likely contributes to pathogen persistence in the host. The exact nature of the residue in PG that is deacetylated has not been determined. Is also able to catalyze the deacetylation of acetylated xylan, and, to a lesser extent, that of chitin and chitosan. Therefore, this enzyme might play a role during infection, considering that xylan-containing carbohydrate structures are among those commonly consumed by humans (By similarity). In vitro, does not show activity on N-acetylglucosamine (GlcNAc), chitotriose (GlcNAc3), some N-acetyl-dipeptides and allantoinase.<ref>PMID:21559431</ref>
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Peptidoglycan deacetlyase (HP0310, HpPgdA) from the gram-negative pathogen Helicobacter pylori, has been indicated as the enzyme responsible for a peptidoglycan modification that counteracts the host immune response. HpPgdA has been cloned, purified and expressed in good yield in E. coli. It has been crystallized, its structure determined and activity tests in vitro performed. The enzyme, which belongs to the polysaccharide deacetylases protein family, is a homo-tetramer. The four polypeptide chains, each folded into a single domain characterized by a non-canonical TIM-barrel fold, are arranged around a four-fold symmetry axis. The active site, one per monomer, contains a heavy ion coordinated in a way similar to other deacetylases. However, the enzyme showed no in vitro activity on the typical polysaccharide substrates of peptidoglycan deacetylases. In striking contrast with the known peptidoglycan deacetylases, HpPgdA does not exhibit a solvent-accessible polysaccharide binding groove, suggesting that the enzyme binds a small molecule at the active site.
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The Structure of Helicobacter pylori HP0310 Reveals an Atypical Peptidoglycan Deacetylase.,Shaik MM, Cendron L, Percudani R, Zanotti G PLoS One. 2011 Apr 29;6(4):e19207. PMID:21559431<ref>PMID:21559431</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3qbu" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Helpg]]
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[[Category: Helicobacter pylori G27]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Cendron, L]]
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[[Category: Cendron L]]
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[[Category: Percudani, R]]
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[[Category: Percudani R]]
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[[Category: Shaik, M M]]
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[[Category: Shaik MM]]
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[[Category: Zanotti, G]]
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[[Category: Zanotti G]]
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[[Category: Deacetylase]]
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[[Category: Hydrolase]]
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[[Category: Metallo enzyme]]
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[[Category: Peptidoglycan]]
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[[Category: Tim barrel]]
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Current revision

Crystal structure of putative peptidoglycan deactelyase (HP0310) from Helicobacter pylori

PDB ID 3qbu

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