2bg8: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
Line 20: | Line 20: | ||
==About this Structure== | ==About this Structure== | ||
2BG8 is a 2 chains structure | 2BG8 is a 2 chains structure with sequences from [http://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BG8 OCA]. | ||
==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]] | ||
Line 33: | Line 33: | ||
[[Category: Antibiotic resistance]] | [[Category: Antibiotic resistance]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 3 08:57:49 2010'' |
Revision as of 09:57, 3 February 2010
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.
Template:ABSTRACT PUBMED 15779910
About this StructureAbout this Structure
2BG8 is a 2 chains structure with sequences 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
Page seeded by OCA on Wed Feb 3 08:57:49 2010