2bg6: Difference between revisions
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[[Image:2bg6.png|left|200px]] | [[Image:2bg6.png|left|200px]] | ||
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{{STRUCTURE_2bg6| PDB=2bg6 | SCENE= }} | {{STRUCTURE_2bg6| PDB=2bg6 | SCENE= }} | ||
=== | ===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.=== | ||
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==About this Structure== | ==About this Structure== | ||
[[2bg6]] is a 2 chain structure of [[Beta-lactamase]] 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=2BG6 OCA]. | |||
==See Also== | |||
*[[Beta-lactamase|Beta-lactamase]] | |||
==Reference== | ==Reference== | ||
<ref group="xtra">PMID: | <ref group="xtra">PMID:015779910</ref><ref group="xtra">PMID:011827530</ref><ref group="xtra">PMID:009730812</ref><references group="xtra"/> | ||
[[Category: Bacillus cereus]] | [[Category: Bacillus cereus]] | ||
[[Category: Beta-lactamase]] | [[Category: Beta-lactamase]] | ||
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[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Metallo-beta-lactamase]] | [[Category: Metallo-beta-lactamase]] | ||
Revision as of 09:59, 20 June 2012
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.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.
Template:ABSTRACT PUBMED 15779910
About this StructureAbout this Structure
2bg6 is a 2 chain structure of Beta-lactamase with sequence from Bacillus cereus. Full crystallographic information is available from OCA.
See AlsoSee Also
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