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| - | [[Image:2blm.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2blm| PDB=2blm | SCENE= }} | | {{STRUCTURE_2blm| PDB=2blm | SCENE= }} |
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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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| - | ==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 |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 2326252 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_2326252}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Knox, J R.]] | | [[Category: Knox, J R.]] |
| | [[Category: Moews, P C.]] | | [[Category: Moews, P C.]] |
| - | ''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 Tue Jul 29 16:05:52 2008'' |
Revision as of 13:05, 29 July 2008
Template:STRUCTURE 2blm
BETA-LACTAMASE OF BACILLUS LICHENIFORMIS 749(SLASH)C AT 2 ANGSTROMS RESOLUTION
Template:ABSTRACT PUBMED 2326252
About this Structure
2BLM is a Single protein structure of sequence from Bacillus licheniformis. Full crystallographic information is available from OCA.
Reference
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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