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| | ==Structure of Bacteriophage poly-gamma-glutamate hydrolase== | | ==Structure of Bacteriophage poly-gamma-glutamate hydrolase== |
| - | <StructureSection load='3a9l' size='340' side='right' caption='[[3a9l]], [[Resolution|resolution]] 1.90Å' scene=''> | + | <StructureSection load='3a9l' size='340' side='right'caption='[[3a9l]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3a9l]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_phage_phinit1 Bacillus phage phinit1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A9L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3A9L FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3a9l]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_phage_phiNIT1 Bacillus phage phiNIT1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A9L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3A9L FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 1.9Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pghP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=207656 Bacillus phage phiNIT1])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3a9l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a9l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3a9l RCSB], [http://www.ebi.ac.uk/pdbsum/3a9l PDBsum]</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=3a9l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a9l OCA], [https://pdbe.org/3a9l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3a9l RCSB], [https://www.ebi.ac.uk/pdbsum/3a9l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3a9l ProSAT]</span></td></tr> |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/Q852V1_9CAUD Q852V1_9CAUD] |
| - | Poly-gamma-glutamate hydrolase P (PghP) of Bacillus subtilis bacteriophage PhiNIT1 hydrolyzes the gamma-glutamyl peptide linkage of extracellular poly-gamma-glutamate produced by bacilli, which facilitates infection and propagation of phage progenies. Crystal structure of PghP was determined at a resolution of 1.9 A. Structure of PghP was elucidated as a globular protein with an open alpha/beta mixed core structure and a seven-stranded parallel/anti-parallel beta-sheet. The beta-sheet contained a core four-stranded parallel beta-sheet. A zinc-binding motif, His-Glu-His, was identified at the C-terminal end of the beta-sheet. Structure analysis demonstrated that PghP, which had not been previously classified into any peptidase/protease family due to lack of amino acid sequence similarity with known enzymes, had a catalytic center containing a zinc ion and an overall topology resembling mammalian carboxypeptidase A and related enzymes. Structural comparisons indicated important amino acid residues of PghP for catalysis and recognition of the gamma-peptide bond of poly-gamma-glutamate, which was confirmed by site-directed mutagenesis of PghP. Proteins 2011. (c) 2012 Wiley Periodicals, Inc.
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| - | Crystal structure of bacteriophage varphiNIT1 zinc peptidase PghP that hydrolyzes gamma-glutamyl linkage of bacterial poly-gamma-glutamate.,Fujimoto Z, Kimura K Proteins. 2012 Mar;80(3):722-32. doi: 10.1002/prot.23229. Epub 2011 Nov 22. PMID:22105902<ref>PMID:22105902</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | == References ==
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| - | <references/>
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus phage phinit1]] | + | [[Category: Bacillus phage phiNIT1]] |
| - | [[Category: Fujimoto, Z]] | + | [[Category: Large Structures]] |
| - | [[Category: Kimura, K]] | + | [[Category: Fujimoto Z]] |
| - | [[Category: Hydrolase]] | + | [[Category: Kimura K]] |
| - | [[Category: Open alpha/beta mixed core structure]]
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| - | [[Category: Zinc ion binding]]
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