2blm: Difference between revisions

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[[Image:2blm.jpg|left|200px]]
[[Image:2blm.jpg|left|200px]]


{{Structure
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-lactamase Beta-lactamase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.6 3.5.2.6] </span>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2blm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2blm OCA], [http://www.ebi.ac.uk/pdbsum/2blm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2blm RCSB]</span>
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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'''
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[[Category: Knox, J R.]]
[[Category: Knox, J R.]]
[[Category: Moews, P C.]]
[[Category: Moews, P C.]]
[[Category: hydrolase(acting in cyclic amides)]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 20:27:44 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:08:15 2008''

Revision as of 20:27, 3 May 2008

File:2blm.jpg

Template:STRUCTURE 2blm

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


OverviewOverview

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.

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 Page seeded by OCA on Sat May 3 20:27:44 2008

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