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| == Function == | | == Function == |
| [https://www.uniprot.org/uniprot/Q852V1_9CAUD Q852V1_9CAUD] | | [https://www.uniprot.org/uniprot/Q852V1_9CAUD Q852V1_9CAUD] |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| 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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| <div class="pdbe-citations 3a9l" style="background-color:#fffaf0;"></div>
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| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
