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==Crystal Structures Of Glutaryl 7-Aminocephalosporanic Acid Acylase: mutational study of activation mechanism== | ==Crystal Structures Of Glutaryl 7-Aminocephalosporanic Acid Acylase: mutational study of activation mechanism== | ||
<StructureSection load='2adv' size='340' side='right' caption='[[2adv]], [[Resolution|resolution]] 2.24Å' scene=''> | <StructureSection load='2adv' size='340' side='right' caption='[[2adv]], [[Resolution|resolution]] 2.24Å' scene=''> | ||
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ae3|2ae3]], [[2ae4|2ae4]], [[2ae5|2ae5]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ae3|2ae3]], [[2ae4|2ae4]], [[2ae5|2ae5]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Penicillin_amidase Penicillin amidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.11 3.5.1.11] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Penicillin_amidase Penicillin amidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.11 3.5.1.11] </span></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=2adv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2adv OCA], [http://pdbe.org/2adv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2adv RCSB], [http://www.ebi.ac.uk/pdbsum/2adv PDBsum]</span></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=2adv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2adv OCA], [http://pdbe.org/2adv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2adv RCSB], [http://www.ebi.ac.uk/pdbsum/2adv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2adv ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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</div> | </div> | ||
<div class="pdbe-citations 2adv" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 2adv" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 19:32, 12 October 2017
Crystal Structures Of Glutaryl 7-Aminocephalosporanic Acid Acylase: mutational study of activation mechanismCrystal Structures Of Glutaryl 7-Aminocephalosporanic Acid Acylase: mutational study of activation mechanism
Structural highlights
Function[G7AC_PSEU7] Catalyzes the deacylation of 7 beta-(4-carboxybutanamido)cephalosporanic acid (glutaryl-7-aminocephalosporanic acid or GL-7-ACA) to 7-aminocephalosporanic acid (7-ACA).[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedCephalosporin acylase (CA), a member of the N-terminal nucleophile hydrolase family, is activated through sequential primary and secondary autoproteolytic reactions with the release of a pro segment. We have determined crystal structures of four CA mutants. Two mutants are trapped after the primary cleavage, and the other two undergo secondary cleavage slowly. These structures provide a look at pro-segment conformation during activation in N-terminal nucleophile hydrolases. The highly strained helical pro segment of precursor is transformed into a relaxed loop in the intermediates, suggesting that the relaxation of structural constraints drives the primary cleavage reaction. The secondary autoproteolytic step has been proposed to be intermolecular. However, our analysis provides evidence that CA is processed in two sequential steps of intramolecular autoproteolysis involving two distinct residues in the active site, the first a serine and the second a glutamate. Insight into autoproteolytic activation from the structure of cephalosporin acylase: a protein with two proteolytic chemistries.,Kim JK, Yang IS, Shin HJ, Cho KJ, Ryu EK, Kim SH, Park SS, Kim KH Proc Natl Acad Sci U S A. 2006 Feb 7;103(6):1732-7. Epub 2006 Jan 30. PMID:16446446[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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