2bg8
BACILLUS CEREUS METALLO-BETA-LACTAMASE (BCII) ARG (121) CYS MUTANT. SOLVED AT PH4.5 USING 20 MICROMOLAR ZNSO4 IN THE BUFFER. 1MM DTT AND 1MM TCEP-HCL WERE USED AS REDUCING AGENTS.BACILLUS CEREUS METALLO-BETA-LACTAMASE (BCII) ARG (121) CYS MUTANT. SOLVED AT PH4.5 USING 20 MICROMOLAR ZNSO4 IN THE BUFFER. 1MM DTT AND 1MM TCEP-HCL WERE USED AS REDUCING AGENTS.
About this StructureAbout this Structure
2bg8 is a 2 chain structure with sequence from Bacillus cereus. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ 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:http://dx.doi.org/10.1021/bi980506i