1bvt: Difference between revisions

Revision as of 19:47, 30 June 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1bvt.png

Template:STRUCTURE 1bvt

METALLO-BETA-LACTAMASE FROM BACILLUS CEREUS 569/H/9METALLO-BETA-LACTAMASE FROM BACILLUS CEREUS 569/H/9

Template:ABSTRACT PUBMED 9761898

About this StructureAbout this Structure

1BVT is a Single protein structure of sequence from Bacillus cereus. This structure supersedes the now removed PDB entry 1bme. Full crystallographic information is available from OCA.

ReferenceReference

1.85 A resolution structure of the zinc (II) beta-lactamase from Bacillus cereus., Carfi A, Duee E, Galleni M, Frere JM, Dideberg O, Acta Crystallogr D Biol Crystallogr. 1998 May 1;54(Pt 3):313-23. PMID:9761898

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OCA

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-'''METALLO-BETA-LACTAMASE FROM BACILLUS CEREUS 569/H/9'''
+===METALLO-BETA-LACTAMASE FROM BACILLUS CEREUS 569/H/9===
-==Overview==
+<!--
-Class B beta-lactamases are wide spectrum enzymes which require bivalent metal ions for activity. The structure of the class B zinc-ion-dependent beta-lactamase from Bacillus cereus (BCII) has been refined at 1.85 A resolution using data collected on cryocooled crystals (100 K). The enzyme from B. cereus has a molecular mass of 24 946 Da and is folded into a beta-sandwich structure with helices on the external faces. The active site is located in a groove running between the two beta-sheets [Carfi et al. (1995). EMBO J. 14, 4914-4921]. The 100 K high-resolution BCII structure shows one fully and one partially occupied zinc sites. The zinc ion in the fully occupied site (the catalytic zinc) is coordinated by three histidines and one water molecule. The second zinc ion is at 3.7 A from the first one and is coordinated by one histidine, one cysteine, one aspartate and one unknown molecule (most likely a carbonate ion). In the B. cereus zinc beta-lactamase the affinity for the second metal-ion is low at the pH of crystallization (Kd = 25 mM, 293 K; [Baldwin et al. (1978). Biochem. J. 175, 441-447] and the dissociation constant of the second zinc ion was thus apparently decreased at the cryogenic temperature. In addition, the structure of the apo enzyme was determined at 2.5 A resolution. The removal of the zinc ion by chelating agents causes small changes in the active-site environment.
+The line below this paragraph, {{ABSTRACT_PUBMED_9761898}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9761898 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_9761898}}
 ==About this Structure==
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 [[Category: Metallo beta-lactamase]]
 [[Category: Zinc]]
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