3a9l: Difference between revisions
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[[ | ==Structure of Bacteriophage poly-gamma-glutamate hydrolase== | ||
<StructureSection load='3a9l' size='340' side='right' caption='[[3a9l]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
== 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> | |||
</td></tr><tr><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><br> | |||
<tr><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><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> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
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[[Category: Bacillus phage phinit1]] | [[Category: Bacillus phage phinit1]] | ||
[[Category: Fujimoto, Z.]] | [[Category: Fujimoto, Z.]] | ||