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New page: left|200px<br /> <applet load="1azw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1azw, resolution 2.7Å" /> '''PROLINE IMINOPEPTIDA...
 
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[[Image:1azw.gif|left|200px]]<br />
<applet load="1azw" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1azw, resolution 2.7&Aring;" />
'''PROLINE IMINOPEPTIDASE FROM XANTHOMONAS CAMPESTRIS PV. CITRI'''<br />


==Overview==
==PROLINE IMINOPEPTIDASE FROM XANTHOMONAS CAMPESTRIS PV. CITRI==
The proline iminopeptidase from Xanthomonas campestris pv. citri is a, serine peptidase that catalyses the removal of N-terminal proline residues, from peptides with high specificity. We have solved its three-dimensional, structure by multiple isomorphous replacement and refined it to a, crystallographic R-factor of 19.2% using X-ray data to 2.7 A resolution., The protein is folded into two contiguous domains. The larger domain shows, the general topology of the alpha/beta hydrolase fold, with a central, eight-stranded beta-sheet flanked by two helices and the 11 N-terminal, residues on one side, and by four helices on the other side. The smaller, domain is placed on top of the larger domain and essentially consists of, six helices. The active site, located at the end of a deep pocket at ... [[http://ispc.weizmann.ac.il/pmbin/getpm?9427736 (full description)]]
<StructureSection load='1azw' size='340' side='right'caption='[[1azw]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1azw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Xanthomonas_citri Xanthomonas citri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AZW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AZW FirstGlance]. <br>
1AZW is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Xanthomonas_smithii_subsp._citri Xanthomonas smithii subsp. citri]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.5 3.4.11.5]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AZW 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]] 2.7&#8491;</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=1azw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1azw OCA], [https://pdbe.org/1azw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1azw RCSB], [https://www.ebi.ac.uk/pdbsum/1azw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1azw ProSAT]</span></td></tr>
==Reference==
</table>
Structure of proline iminopeptidase from Xanthomonas campestris pv. citri: a prototype for the prolyl oligopeptidase family., Medrano FJ, Alonso J, Garcia JL, Romero A, Bode W, Gomis-Ruth FX, EMBO J. 1998 Jan 2;17(1):1-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9427736 9427736]
== Function ==
[[Category: Single protein]]
[https://www.uniprot.org/uniprot/PIP_XANCI PIP_XANCI] May be involved in proline metabolism and sensitivity to ascamycin. Has ascamycin dealanylating activity.
[[Category: Xanthomonas smithii subsp. citri]]
== Evolutionary Conservation ==
[[Category: Alonso, J.]]
[[Image:Consurf_key_small.gif|200px|right]]
[[Category: Bode, W.]]
Check<jmol>
[[Category: Garcia, J.L.]]
  <jmolCheckbox>
[[Category: Gomis-Ruth, F.X.]]
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/az/1azw_consurf.spt"</scriptWhenChecked>
[[Category: Medrano, F.J.]]
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
[[Category: Romero, A.]]
    <text>to colour the structure by Evolutionary Conservation</text>
[[Category: aminopeptidase]]
  </jmolCheckbox>
[[Category: proline iminopeptidase]]
</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=1azw ConSurf].
[[Category: serine protease]]
<div style="clear:both"></div>
[[Category: xanthomonas campestris]]
__TOC__
 
</StructureSection>
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 21:32:18 2007''
[[Category: Large Structures]]
[[Category: Xanthomonas citri]]
[[Category: Alonso J]]
[[Category: Bode W]]
[[Category: Garcia JL]]
[[Category: Gomis-Ruth FX]]
[[Category: Medrano FJ]]
[[Category: Romero A]]

Latest revision as of 06:34, 7 February 2024

PROLINE IMINOPEPTIDASE FROM XANTHOMONAS CAMPESTRIS PV. CITRI

1azw, resolution 2.70Å

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