2adv: Difference between revisions

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OCA

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 <StructureSection load='2adv' size='340' side='right'caption='[[2adv]], [[Resolution|resolution]] 2.24&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2adv]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_sp._gk-16 Pseudomonas sp. gk-16]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ADV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ADV FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2adv]] is a 3 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=2ADV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ADV FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2ae3|2ae3]], [[2ae4|2ae4]], [[2ae5|2ae5]]</div></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]] 2.244&#8491;</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Penicillin_amidase Penicillin amidase], with EC number [https://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'>[https://proteopedia.org/fgij/fg.htm?mol=2adv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2adv OCA], [https://pdbe.org/2adv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2adv RCSB], [https://www.ebi.ac.uk/pdbsum/2adv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2adv ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/G7AC_PSEU7 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).<ref>PMID:2993240</ref>
+[https://www.uniprot.org/uniprot/G7AC_PSEU7 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).<ref>PMID:2993240</ref>
 == Evolutionary Conservation ==
 [[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=2adv ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Cephalosporin 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<ref>PMID:16446446</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 2adv" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 37: / Line 27: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Penicillin amidase]]
+[[Category: Pseudomonas sp. GK16]]
-[[Category: Pseudomonas sp. gk-16]]
+[[Category: Cho KJ]]
-[[Category: Cho, K J]]
+[[Category: Kim JK]]
-[[Category: Kim, J K]]
+[[Category: Kim KH]]
-[[Category: Kim, K H]]
+[[Category: Kim SH]]
-[[Category: Kim, S H]]
+[[Category: Park SS]]
-[[Category: Park, S S]]
+[[Category: Ryu EK]]
-[[Category: Ryu, E K]]
+[[Category: Shin HJ]]
-[[Category: Shin, H J]]
+[[Category: Yang IS]]
-[[Category: Yang, I S]]
-[[Category: Autoproteolysis]]
-[[Category: Cephalosporin acylase]]
-[[Category: Hydrolase]]
-[[Category: Intermediate structure]]
-[[Category: Precursor activation]]