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<StructureSection load='1ilw' size='340' side='right'caption='[[1ilw]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
<StructureSection load='1ilw' size='340' side='right'caption='[[1ilw]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1ilw]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/'pyrococcus_shinkaii' 'pyrococcus shinkaii']. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ILW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ILW FirstGlance]. <br>
<table><tr><td colspan='2'>[[1ilw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ILW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ILW FirstGlance]. <br>
</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hydrolase Hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.19 3.5.1.19] </span></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]] 2.05&#8491;</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=1ilw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ilw OCA], [http://pdbe.org/1ilw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ilw RCSB], [http://www.ebi.ac.uk/pdbsum/1ilw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ilw ProSAT], [http://www.topsan.org/Proteins/BSGC/1ilw TOPSAN]</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=1ilw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ilw OCA], [https://pdbe.org/1ilw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ilw RCSB], [https://www.ebi.ac.uk/pdbsum/1ilw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ilw ProSAT], [https://www.topsan.org/Proteins/BSGC/1ilw TOPSAN]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/O58727_PYRHO O58727_PYRHO]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ilw ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ilw ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Bacterial pyrazinamidase (PZAase)/nicotinamidase converts pyrazinamide (PZA) to ammonia and pyrazinoic acid, which is active against Mycobacterium tuberculosis. Loss of PZAase activity is the major mechanism of pyrazinamide-resistance by M. tuberculosis. We have determined the crystal structure of the gene product of Pyrococcus horikoshii 999 (PH999), a PZAase, and its complex with zinc ion by X-ray crystallography. The overall fold of PH999 is similar to that of N-carbamoylsarcosine amidohydrolase (CSHase) of Arthrobacter sp. and YcaC of Escherichia coli, a protein with unknown physiological function. The active site of PH999 was identified by structural features that are also present in the active sites of CSHase and YcaC: a triad (D10, K94, and C133) and a cis-peptide (between V128 and A129). Surprisingly, a metal ion-binding site was revealed in the active site and subsequently confirmed by crystal structure of PH999 in complex with Zn(2+). The roles of the triad, cis-peptide, and metal ion in the catalysis are proposed. Because of extensive homology between PH999 and PZAase of M. tuberculosis (37% sequence identity), the structure of PH999 provides a structural basis for understanding PZA-resistance by M. tuberculosis harboring PZAase mutations.
Crystal structure and mechanism of catalysis of a pyrazinamidase from Pyrococcus horikoshii.,Du X, Wang W, Kim R, Yakota H, Nguyen H, Kim SH Biochemistry. 2001 Nov 27;40(47):14166-72. PMID:11714269<ref>PMID:11714269</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1ilw" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Pyrococcus shinkaii]]
[[Category: Hydrolase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Structural genomic]]
[[Category: Pyrococcus horikoshii]]
[[Category: Du, X]]
[[Category: Du X]]
[[Category: Kim, S H]]
[[Category: Kim S-H]]
[[Category: Amidase]]
[[Category: Bsgc structure funded by nih]]
[[Category: Cysteine hydrolase]]
[[Category: Nicotinamidase]]
[[Category: PSI, Protein structure initiative]]
[[Category: Pyrazinamidase]]
[[Category: Pyrazinamide]]
[[Category: Tuberculosis]]
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