2ae3: Difference between revisions

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<StructureSection load='2ae3' size='340' side='right'caption='[[2ae3]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='2ae3' size='340' side='right'caption='[[2ae3]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2ae3]] is a 2 chain structure with sequence from [http://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=2AE3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2AE3 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2ae3]] 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=2AE3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AE3 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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]] 2.4&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2adv|2adv]], [[2ae4|2ae4]], [[2ae5|2ae5]]</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='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'>[https://proteopedia.org/fgij/fg.htm?mol=2ae3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ae3 OCA], [https://pdbe.org/2ae3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ae3 RCSB], [https://www.ebi.ac.uk/pdbsum/2ae3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ae3 ProSAT]</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=2ae3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ae3 OCA], [http://pdbe.org/2ae3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ae3 RCSB], [http://www.ebi.ac.uk/pdbsum/2ae3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ae3 ProSAT]</span></td></tr>
</table>
</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>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[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=2ae3 ConSurf].
</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=2ae3 ConSurf].
<div style="clear:both"></div>
<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 2ae3" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[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]]

Latest revision as of 16:40, 13 March 2024

Glutaryl 7-Aminocephalosporanic Acid Acylase: mutational study of activation mechanismGlutaryl 7-Aminocephalosporanic Acid Acylase: mutational study of activation mechanism

Structural highlights

2ae3 is a 2 chain structure with sequence from Pseudomonas sp. GK16. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.4Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

See Also

References

  1. ↑ Matsuda A, Komatsu KI. Molecular cloning and structure of the gene for 7 beta-(4-carboxybutanamido)cephalosporanic acid acylase from a Pseudomonas strain. J Bacteriol. 1985 Sep;163(3):1222-8. PMID:2993240

2ae3, resolution 2.40Å

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OCA
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