2bfk: Difference between revisions
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==Reference== | ==Reference== | ||
<ref group="xtra">PMID:15779910</ref><references group="xtra"/> | <ref group="xtra">PMID:15779910</ref><ref group="xtra">PMID:11827530</ref><ref group="xtra">PMID:9730812</ref><references group="xtra"/> | ||
[[Category: Bacillus cereus]] | [[Category: Bacillus cereus]] | ||
[[Category: Beta-lactamase]] | [[Category: Beta-lactamase]] | ||
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[[Category: Zinc]] | [[Category: Zinc]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Sep 3 16:23:29 2009'' | ||
Revision as of 13:23, 3 September 2009
BACILLUS CEREUS METALLO-BETA-LACTAMASE (BCII) ARG (121) CYS MUTANT. SOLVED AT PH7 USING 20MM ZNSO4 IN BUFFER. 1MM DTT WAS USED AS A REDUCING AGENT
Template:ABSTRACT PUBMED 15779910
About this Structure
2BFK is a 2 chains structure of sequences from Bacillus cereus. Full crystallographic information is available from OCA.
Reference
- Davies AM, Rasia RM, Vila AJ, Sutton BJ, Fabiane SM. Effect of pH on the active site of an Arg121Cys mutant of the metallo-beta-lactamase from Bacillus cereus: implications for the enzyme mechanism. Biochemistry. 2005 Mar 29;44(12):4841-9. PMID:15779910 doi:10.1021/bi047709t
- Rasia RM, Vila AJ. Exploring the role and the binding affinity of a second zinc equivalent in B. cereus metallo-beta-lactamase. Biochemistry. 2002 Feb 12;41(6):1853-60. PMID:11827530
- Fabiane SM, Sohi MK, Wan T, Payne DJ, Bateson JH, Mitchell T, Sutton BJ. Crystal structure of the zinc-dependent beta-lactamase from Bacillus cereus at 1.9 A resolution: binuclear active site with features of a mononuclear enzyme. Biochemistry. 1998 Sep 8;37(36):12404-11. PMID:9730812 doi:https://dx.doi.org/10.1021/bi980506i
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