2blm: Difference between revisions

Revision as of 16:05, 29 July 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:2blm.png

Template:STRUCTURE 2blm

BETA-LACTAMASE OF BACILLUS LICHENIFORMIS 749(SLASH)C AT 2 ANGSTROMS RESOLUTIONBETA-LACTAMASE OF BACILLUS LICHENIFORMIS 749(SLASH)C AT 2 ANGSTROMS RESOLUTION

Template:ABSTRACT PUBMED 2326252

About this StructureAbout this Structure

2BLM is a Single protein structure of sequence from Bacillus licheniformis. Full crystallographic information is available from OCA.

ReferenceReference

Beta-lactamase of Bacillus licheniformis 749/C at 2 A resolution., Moews PC, Knox JR, Dideberg O, Charlier P, Frere JM, Proteins. 1990;7(2):156-71. PMID:2326252

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OCA

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-'''BETA-LACTAMASE OF BACILLUS LICHENIFORMIS 749(SLASH)C AT 2 ANGSTROMS RESOLUTION'''
+===BETA-LACTAMASE OF BACILLUS LICHENIFORMIS 749(SLASH)C AT 2 ANGSTROMS RESOLUTION===
-==Overview==
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-Two crystal forms (A and B) of the 29,500 Da Class A beta-lactamase (penicillinase) from Bacillus licheniformis 749/C have been examined crystallographically. The structure of B-form crystals has been solved to 2 A resolution, the starting model for which was a 3.5 A structure obtained from A-form crystals. The beta-lactamase has an alpha + beta structure with 11 helices and 5 beta-strands seen also in a penicillin target DD-peptidase of Streptomyces R61. Atomic parameters of the two molecules in the asymmetric unit were refined by simulated annealing at 2.0 A resolution. The R factor is 0.208 for the 27,330 data greater than 3 sigma (F), with water molecules excluded from the model. The catalytic Ser-70 is at the N-terminus of a helix and is within hydrogen bonding distance of conserved Lys-73. Also interacting with the Lys-73 are Asn-132 and the conserved Glu-166, which is on a potentially flexible helix-containing loop. The structure suggests the binding of beta-lactam substrates is facilitated by interactions with Lys-234, Thr-235, and Ala-237 in a conserved beta-strand peptide, which is antiparallel to the beta-lactam's acylamido linkage; an exposed cavity near Asn-170 exists for acylamido substituents. The reactive double bond of clavulanate-type inhibitors may interact with Arg-244 on the fourth beta-strand. A very similar binding site architecture is seen in the DD-peptidase.
+The line below this paragraph, {{ABSTRACT_PUBMED_2326252}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_2326252}}
 ==About this Structure==
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 [[Category: Knox, J R.]]
 [[Category: Moews, P C.]]
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