2bg6
From Proteopedia
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==About this Structure== | ==About this Structure== | ||
| - | 2BG6 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, SO4, AZI and GOL as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ | + | 2BG6 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, SO4, AZI and GOL as [[http://en.wikipedia.org/wiki/ligands ligands]]. 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: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BG6 OCA]]. |
==Reference== | ==Reference== | ||
Effect of pH on the active site of an Arg121Cys mutant of the metallo-beta-lactamase from Bacillus cereus: implications for the enzyme mechanism., Davies AM, Rasia RM, Vila AJ, Sutton BJ, Fabiane SM, Biochemistry. 2005 Mar 29;44(12):4841-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15779910 15779910] | Effect of pH on the active site of an Arg121Cys mutant of the metallo-beta-lactamase from Bacillus cereus: implications for the enzyme mechanism., Davies AM, Rasia RM, Vila AJ, Sutton BJ, Fabiane SM, Biochemistry. 2005 Mar 29;44(12):4841-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15779910 15779910] | ||
[[Category: Bacillus cereus]] | [[Category: Bacillus cereus]] | ||
| + | [[Category: Beta-lactamase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Davies, A.M.]] | [[Category: Davies, A.M.]] | ||
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[[Category: zinc]] | [[Category: zinc]] | ||
| - | ''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 10:44:36 2007'' |
Revision as of 08:39, 30 October 2007
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BACILLUS CEREUS METALLO-BETA-LACTAMASE (BCII) ARG (121) CYS MUTANT. SOLVED AT PH5 USING 20 MICROMOLAR ZNSO4 IN THE BUFFER. 1MM DTT WAS USED AS A REDUCING AGENT. CYS221 IS OXIDIZED.
Overview
The zinc-dependent metallo-beta-lactamases are a group of bacterial, enzymes that pose a threat to the future efficacy of present-day, antibiotics. Their mechanism is poorly understood, and there are no, clinically useful inhibitors. While most members of the group contain two, tightly bound zinc ions in their active sites, the Bacillus cereus enzyme, has a much lower affinity for its second zinc (Zn2), thought to be due to, the presence of Arg121 immediately beneath the floor of the active site, (cf. Cys/Ser/His121 in the bizinc enzymes). Crystal structures of the, Arg121Cys mutant of the B. cereus 569/H/9 enzyme were solved at pH 7.0, 5.0, and 4.5, each in the presence of either 20 microM or 20 mM Zn(2+) to, generate the mono- and bizinc forms, respectively. Surprisingly, the, structure ... [(full description)]
About this Structure
2BG6 is a [Single protein] structure of sequence from [Bacillus cereus] with ZN, SO4, AZI and GOL as [ligands]. Active as [Beta-lactamase], with EC number [3.5.2.6]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Effect of pH on the active site of an Arg121Cys mutant of the metallo-beta-lactamase from Bacillus cereus: implications for the enzyme mechanism., Davies AM, Rasia RM, Vila AJ, Sutton BJ, Fabiane SM, Biochemistry. 2005 Mar 29;44(12):4841-9. PMID:15779910
Page seeded by OCA on Tue Oct 30 10:44:36 2007
Categories: Bacillus cereus | Beta-lactamase | Single protein | Davies, A.M. | Fabiane, S.M. | Rasia, R.M. | Sutton, B.J. | Vila, A.J. | AZI | GOL | SO4 | ZN | Antibiotic resistance | Hydrolase | Metallo-beta-lactamase | Zinc
