2bga
From Proteopedia
(Difference between revisions)
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| - | {{Seed}} | ||
[[Image:2bga.png|left|200px]] | [[Image:2bga.png|left|200px]] | ||
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==About this Structure== | ==About this Structure== | ||
| - | + | [[2bga]] is a 2 chain structure with sequence 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=2BGA 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]] | ||
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[[Category: Metallo-beta-lactamase]] | [[Category: Metallo-beta-lactamase]] | ||
[[Category: Zinc]] | [[Category: Zinc]] | ||
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 18:16:39 2009'' | ||
Revision as of 21:12, 14 March 2011
BACILLUS CEREUS METALLO-BETA-LACTAMASE (BCII) ARG (121) CYS MUTANT. SOLVED AT PH7 USING 20 MICROMOLAR ZNSO4 IN THE BUFFER. 1MM DTT WAS USED AS A REDUCING AGENT. CYS221 IS OXIDIZED.
Template:ABSTRACT PUBMED 15779910
About this Structure
2bga is a 2 chain structure with sequence 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:http://dx.doi.org/10.1021/bi980506i
