1jw0: Difference between revisions
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==Structure of cephalosporin acylase in complex with glutarate== | ==Structure of cephalosporin acylase in complex with glutarate== | ||
<StructureSection load='1jw0' size='340' side='right' caption='[[1jw0]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='1jw0' size='340' side='right'caption='[[1jw0]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1jw0]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aj_2067 Aj 2067]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JW0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JW0 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1jw0]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aj_2067 Aj 2067]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JW0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JW0 FirstGlance]. <br> | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jw/1jw0_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jw/1jw0_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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</div> | </div> | ||
<div class="pdbe-citations 1jw0" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1jw0" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Cephalosporin acylase|Cephalosporin acylase]] | |||
*[[Cephalosporin acylase 3D structures|Cephalosporin acylase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Aj 2067]] | [[Category: Aj 2067]] | ||
[[Category: Large Structures]] | |||
[[Category: Hol, W G.J]] | [[Category: Hol, W G.J]] | ||
[[Category: Kim, Y]] | [[Category: Kim, Y]] | ||
Revision as of 16:22, 17 July 2019
Structure of cephalosporin acylase in complex with glutarateStructure of cephalosporin acylase in complex with glutarate
Structural highlights
Function[G7AC_BREDI] Catalyzes the deacylation of 7 beta-(4-carboxybutanamido)cephalosporanic acid (glutaryl-7-aminocephalosporanic acid or GL-7-ACA) to 7-aminocephalosporanic acid (7-ACA). Can not efficiently use cephalosporin C (CPC), penicillin G, or ampicillin as substrates.[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 PubMedBACKGROUND: Semisynthetic cephalosporins are primarily synthesized from 7-aminocephalosporanic acid (7-ACA), which is obtained by environmentally toxic chemical deacylation of cephalosporin C (CPC). Thus, the enzymatic conversion of CPC to 7-ACA by cephalosporin acylase (CA) would be of great interest. However, CAs use glutaryl-7-ACA (GL-7-ACA) as a primary substrate and the enzyme has low turnover rates for CPC. RESULTS: The binary complex structures of CA with GL-7-ACA and glutarate (the side-chain of GL-7-ACA) show extensive interactions between the glutaryl moiety of GL-7-ACA and the seven residues that form the side-chain pocket. These interactions explain why the D-alpha-aminoadipyl side-chain of CPC yields a poorer substrate than GL-7-ACA. CONCLUSIONS: This understanding of the nature of substrate specificity may be useful in the design of an enzyme with an improved performance for the conversion of CPC to 7-ACA. Additionally, the catalytic mechanism of the deacylation reaction was revealed by the ligand bound structures. Structure of cephalosporin acylase in complex with glutaryl-7-aminocephalosporanic acid and glutarate: insight into the basis of its substrate specificity.,Kim Y, Hol WG Chem Biol. 2001 Dec;8(12):1253-64. PMID:11755403[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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