1gkf
From Proteopedia
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==About this Structure== | ==About this Structure== | ||
| - | 1GKF is a [[http://en.wikipedia.org/wiki/Protein_complex Protein complex]] structure of sequences from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]] with CA and EDO as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ | + | 1GKF is a [[http://en.wikipedia.org/wiki/Protein_complex Protein complex]] structure of sequences from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]] with CA and EDO as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[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]]. Structure known Active Site: CA. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GKF OCA]]. |
==Reference== | ==Reference== | ||
Crystal structures of penicillin acylase enzyme-substrate complexes: structural insights into the catalytic mechanism., McVey CE, Walsh MA, Dodson GG, Wilson KS, Brannigan JA, J Mol Biol. 2001 Oct 12;313(1):139-50. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11601852 11601852] | Crystal structures of penicillin acylase enzyme-substrate complexes: structural insights into the catalytic mechanism., McVey CE, Walsh MA, Dodson GG, Wilson KS, Brannigan JA, J Mol Biol. 2001 Oct 12;313(1):139-50. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11601852 11601852] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
| + | [[Category: Penicillin amidase]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Brannigan, J.A.]] | [[Category: Brannigan, J.A.]] | ||
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[[Category: antibiotic resistance]] | [[Category: antibiotic resistance]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 10:24:17 2007'' |
Revision as of 08:19, 30 October 2007
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CRYSTAL STRUCTURES OF PENICILLIN ACYLASE ENZYME-SUBSTRATE COMPLEXES: STRUCTURAL INSIGHTS INTO THE CATALYTIC MECHANISM
Overview
The crystal structure of penicillin G acylase from Escherichia coli has, been determined to a resolution of 1.3 A from a crystal form grown in the, presence of ethylene glycol. To study aspects of the substrate specificity, and catalytic mechanism of this key biotechnological enzyme, mutants were, made to generate inactive protein useful for producing enzyme-substrate, complexes. Owing to the intimate association of enzyme activity and, precursor processing in this protein family (the Ntn hydrolases), most, attempts to alter active-site residues lead to processing defects., Mutation of the invariant residue Arg B263 results in the accumulation of, a protein precursor form. However, the mutation of Asn B241, a residue, implicated in stabilisation of the tetrahedral intermediate during, ... [(full description)]
About this Structure
1GKF is a [Protein complex] structure of sequences from [Escherichia coli] with CA and EDO as [ligands]. Active as [Penicillin amidase], with EC number [3.5.1.11]. Structure known Active Site: CA. Full crystallographic information is available from [OCA].
Reference
Crystal structures of penicillin acylase enzyme-substrate complexes: structural insights into the catalytic mechanism., McVey CE, Walsh MA, Dodson GG, Wilson KS, Brannigan JA, J Mol Biol. 2001 Oct 12;313(1):139-50. PMID:11601852
Page seeded by OCA on Tue Oct 30 10:24:17 2007
