1fm2
From Proteopedia
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| - | [[Image:1fm2.jpg|left|200px]] | + | [[Image:1fm2.jpg|left|200px]] |
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| - | '''THE 2 ANGSTROM CRYSTAL STRUCTURE OF CEPHALOSPORIN ACYLASE''' | + | {{Structure |
| + | |PDB= 1fm2 |SIZE=350|CAPTION= <scene name='initialview01'>1fm2</scene>, resolution 2.0Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''THE 2 ANGSTROM CRYSTAL STRUCTURE OF CEPHALOSPORIN ACYLASE''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1FM2 is a [ | + | 1FM2 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Brevundimonas_diminuta Brevundimonas diminuta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FM2 OCA]. |
==Reference== | ==Reference== | ||
| - | The 2.0 A crystal structure of cephalosporin acylase., Kim Y, Yoon K, Khang Y, Turley S, Hol WG, Structure. 2000 Oct 15;8(10):1059-68. PMID:[http:// | + | The 2.0 A crystal structure of cephalosporin acylase., Kim Y, Yoon K, Khang Y, Turley S, Hol WG, Structure. 2000 Oct 15;8(10):1059-68. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11080627 11080627] |
[[Category: Brevundimonas diminuta]] | [[Category: Brevundimonas diminuta]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: Turley, S.]] | [[Category: Turley, S.]] | ||
[[Category: Yoon, K H.]] | [[Category: Yoon, K H.]] | ||
| - | [[Category: | + | [[Category: antibiotic]] |
[[Category: cephalosporin acylase]] | [[Category: cephalosporin acylase]] | ||
[[Category: n-terminal hydrolase]] | [[Category: n-terminal hydrolase]] | ||
[[Category: penicillin acylase]] | [[Category: penicillin acylase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:10:54 2008'' |
Revision as of 09:10, 20 March 2008
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| , resolution 2.0Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE 2 ANGSTROM CRYSTAL STRUCTURE OF CEPHALOSPORIN ACYLASE
Overview
BACKGROUND: Semisynthetic cephalosporins are primarily synthesized from 7-aminocephalosporanic acid (7-ACA), which is usually obtained by chemical deacylation of cephalosporin C (CPC). The chemical production of 7-ACA includes, however, several expensive steps and requires thorough treatment of chemical wastes. Therefore, an enzymatic conversion of CPC to 7-ACA by cephalosporin acylase is of great interest. The biggest obstacle preventing this in industrial production is that cephalosporin acylase uses glutaryl-7ACA as a primary substrate and has low substrate specificity for CPC. RESULTS: We have solved the first crystal structure of a cephalosporin acylase from Pseudomonas diminuta at 2.0 A resolution. The overall structure looks like a bowl with two "knobs" consisting of helix- and strand-rich regions, respectively. The active site is mostly formed by the distinctive structural motif of the N-terminal (Ntn) hydrolase superfamily. Superposition of the 61 residue active-site pocket onto that of penicillin G acylase shows an rmsd in Calpha positions of 1.38 A. This indicates structural similarity in the active site between these two enzymes, but their overall structures are elsewhere quite different. CONCLUSION: The substrate binding pocket of the P. diminuta cephalosporin acylase provides detailed insight into the ten key residues responsible for the specificity of the cephalosporin C side chain in four classes of cephalosporin acylases, and it thereby forms a basis for the design of an enzyme with an improved conversion rate of CPC to 7-ACA. The structure also provides structural evidence that four of the five different classes of cephalosporin acylases can be grouped into one family of the Ntn hydrolase superfamily.
About this Structure
1FM2 is a Protein complex structure of sequences from Brevundimonas diminuta. Full crystallographic information is available from OCA.
Reference
The 2.0 A crystal structure of cephalosporin acylase., Kim Y, Yoon K, Khang Y, Turley S, Hol WG, Structure. 2000 Oct 15;8(10):1059-68. PMID:11080627
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