3qbu
From Proteopedia
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| - | {{STRUCTURE_3qbu| PDB=3qbu | SCENE= }} | ||
| - | ===Crystal structure of putative peptidoglyacn deactelyase (HP0310) from Helicobacter pylori=== | ||
| - | {{ABSTRACT_PUBMED_21559431}} | ||
| - | == | + | ==Crystal structure of putative peptidoglycan deactelyase (HP0310) from Helicobacter pylori== |
| - | [[3qbu]] is a 4 chain structure with sequence from [ | + | <StructureSection load='3qbu' size='340' side='right'caption='[[3qbu]], [[Resolution|resolution]] 2.57Å' scene=''> |
| - | + | == Structural highlights == | |
| - | == | + | <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> |
| - | < | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5701Å</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> |
| - | [ | + | <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> |
| - | [ | + | == Function == |
| - | [[Category: | + | [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> |
| - | [[Category: | + | == References == |
| - | [[Category: | + | <references/> |
| - | [[Category: | + | __TOC__ |
| - | [[Category: | + | </StructureSection> |
| - | [[Category: | + | [[Category: Helicobacter pylori G27]] |
| + | [[Category: Large Structures]] | ||
| + | [[Category: Cendron L]] | ||
| + | [[Category: Percudani R]] | ||
| + | [[Category: Shaik MM]] | ||
| + | [[Category: Zanotti G]] | ||
Current revision
Crystal structure of putative peptidoglycan deactelyase (HP0310) from Helicobacter pylori
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