View source for 3jtq


==Mutations in Cephalosporin Acylase Affecting Stability and Autoproteolysis==
<StructureSection load='3jtq' size='340' side='right'caption='[[3jtq]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3jtq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_sp._GK16 Pseudomonas sp. GK16]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JTQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3JTQ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=3jtq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jtq OCA], [https://pdbe.org/3jtq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3jtq RCSB], [https://www.ebi.ac.uk/pdbsum/3jtq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3jtq ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A4ZVL3_PSEU7 A4ZVL3_PSEU7] 
== 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/jt/3jtq_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=3jtq ConSurf].
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== Publication Abstract from PubMed ==
Cephalosporin acylase (CA), a member of the N-terminal nucleophile hydrolase family, is activated through two steps of intramolecular autoproteolysis, the first mediated by a serine residue, and the second by a glutamate, which releases the pro-segment and produces an active enzyme. In this study, we have determined the crystal structures of mutants which could affect primary or secondary auto-cleavage and of sequential intermediates of a slow-processing mutant at 2.0-2.5A resolutions. The pro-segments of the mutants undergo dynamic conformational changes during activation and adopt surprisingly different loop conformations from one another. However, the autoproteolytic site was found to form a catalytically competent conformation with a solvent water molecule, which was essentially conserved in the CA mutants.

Structural features of cephalosporin acylase reveal the basis of autocatalytic activation.,Cho KJ, Kim JK, Lee JH, Shin HJ, Park SS, Kim KH Biochem Biophys Res Commun. 2009 Dec 11;390(2):342-8. Epub 2009 Oct 2. PMID:19800869<ref>PMID:19800869</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 3jtq" style="background-color:#fffaf0;"></div>

==See Also==
*[[Cephalosporin acylase 3D structures|Cephalosporin acylase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas sp. GK16]]
[[Category: Cho KJ]]
[[Category: Kim JK]]
[[Category: Kim KH]]
[[Category: Lee JH]]
[[Category: Park SS]]
[[Category: Shin HJ]]