1cp9
From Proteopedia
| Line 27: | Line 27: | ||
[[Category: penicillin binding protein]] | [[Category: penicillin binding protein]] | ||
| - | ''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 14:59:36 2007'' |
Revision as of 12:54, 30 October 2007
|
CRYSTAL STRUCTURE OF PENICILLIN G ACYLASE FROM THE BRO1 MUTANT STRAIN OF PROVIDENCIA RETTGERI
Overview
Penicillin G acylase is an important enzyme in the commercial production, of semisynthetic penicillins used to combat bacterial infections. Mutant, strains of Providencia rettgeri were generated from wild-type cultures, subjected to nutritional selective pressure. One such mutant, Bro1, was, able to use 6-bromohexanamide as its sole nitrogen source. Penicillin, acylase from the Bro1 strain exhibited an altered substrate specificity, consistent with the ability of the mutant to process 6-bromohexanamide., The X-ray structure determination of this enzyme was undertaken to, understand its altered specificity and to help in the design of, site-directed mutants with desired specificities. In this paper, the, structure of the Bro1 penicillin G acylase has been solved at 2.5 A, resolution by ... [(full description)]
About this Structure
1CP9 is a [Protein complex] structure of sequences from [Providencia rettgeri] with CA and SO4 as [ligands]. Active as [Penicillin amidase], with EC number [3.5.1.11]. Structure known Active Site: AS. Full crystallographic information is available from [OCA].
Reference
Crystal structure of penicillin G acylase from the Bro1 mutant strain of Providencia rettgeri., McDonough MA, Klei HE, Kelly JA, Protein Sci. 1999 Oct;8(10):1971-81. PMID:10548042
Page seeded by OCA on Tue Oct 30 14:59:36 2007
