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New page: left|200px<br /><applet load="1im5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1im5, resolution 1.65Å" /> '''Crystal Structure of...
 
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[[Image:1im5.jpg|left|200px]]<br /><applet load="1im5" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1im5, resolution 1.65&Aring;" />
'''Crystal Structure of Pyrazinamidase of Pyrococcus horikoshii in Complex with Zinc'''<br />


==Overview==
==Crystal Structure of Pyrazinamidase of Pyrococcus horikoshii in Complex with Zinc==
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.
<StructureSection load='1im5' size='340' side='right'caption='[[1im5]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1im5]] 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=1IM5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IM5 FirstGlance]. <br>
1IM5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Nicotinamidase Nicotinamidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.19 3.5.1.19] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IM5 OCA].
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65&#8491;</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>
==Reference==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1im5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1im5 OCA], [https://pdbe.org/1im5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1im5 RCSB], [https://www.ebi.ac.uk/pdbsum/1im5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1im5 ProSAT]</span></td></tr>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11714269 11714269]
</table>
[[Category: Nicotinamidase]]
== Function ==
[https://www.uniprot.org/uniprot/O58727_PYRHO O58727_PYRHO]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/im/1im5_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1im5 ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pyrococcus horikoshii]]
[[Category: Pyrococcus horikoshii]]
[[Category: Single protein]]
[[Category: Du X]]
[[Category: Du, X.]]
[[Category: Kim S-H]]
[[Category: Kim, S.H.]]
[[Category: ZN]]
[[Category: amidase]]
[[Category: covalent catalysis]]
[[Category: cysteine hydrolase]]
[[Category: drug resistance]]
[[Category: hydrolase]]
[[Category: metal ion catalysis]]
[[Category: nicotinamidase]]
[[Category: pyrazinamidase]]
[[Category: pyrazinamide]]
[[Category: pza resistance]]
[[Category: tuberculosis]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 22:12:42 2007''
Retrieved from "https://proteopedia.org/1im5"