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1bmc
From Proteopedia
(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 ...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1BMC is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus]] with ZN as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.6 3.5.2.6]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BMC OCA]]. | + | 1BMC is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus]] with ZN as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/Beta-lactamase Beta-lactamase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.6 3.5.2.6]]. Structure known Active Site: ZN. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BMC OCA]]. |
==Reference== | ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7588620 7588620] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7588620 7588620] | ||
[[Category: Bacillus cereus]] | [[Category: Bacillus cereus]] | ||
| + | [[Category: Beta-lactamase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Carfi, A.]] | [[Category: Carfi, A.]] | ||
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[[Category: signal]] | [[Category: signal]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 12:06:18 2007'' |
Revision as of 10:01, 30 October 2007
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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 [Beta-lactamase], with EC number [3.5.2.6]. Structure known Active Site: ZN. 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
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