This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1bmc
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /> <applet load="1bmc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bmc, resolution 2.5Å" /> '''STRUCTURE OF A ZINC ...)
Next diff →
Revision as of 16:44, 29 October 2007
|
STRUCTURE OF A ZINC METALLO-BETA-LACTAMASE FROM BACILLUS CEREUS
Overview
The 3-D structure of Bacillus cereus (569/H/9) beta-lactamase (EC, 3.5.2.6), which catalyses the hydrolysis of nearly all beta-lactams, has, been solved at 2.5 A resolution by the multiple isomorphous replacement, method, with density modification and phase combination, from crystals of, the native protein and of a specially designed mutant (T97C). The current, model includes 212 of the 227 amino acid residues, the zinc ion and 10, water molecules. The protein is folded into a beta beta sandwich with, helices on each external face. To our knowledge, this fold has never been, observed. An approximate internal molecular symmetry is found, with a, 2-fold axis passing roughly through the zinc ion and suggesting a possible, gene duplication. The active site is located at one edge of the beta ... [(full description)]
About this Structure
1BMC is a [Single protein] structure of sequence from [Bacillus cereus] with ZN as [ligand]. Active as [[1]], with EC number [3.5.2.6]. Full crystallographic information is available from [OCA].
Reference
The 3-D structure of a zinc metallo-beta-lactamase from Bacillus cereus reveals a new type of protein fold., Carfi A, Pares S, Duee E, Galleni M, Duez C, Frere JM, Dideberg O, EMBO J. 1995 Oct 16;14(20):4914-21. PMID:7588620
Page seeded by OCA on Mon Oct 29 18:48:53 2007
