1e25
From Proteopedia
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| - | [[Image:1e25.gif|left|200px]] | + | [[Image:1e25.gif|left|200px]] |
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| - | '''THE HIGH RESOLUTION STRUCTURE OF PER-1 CLASS A BETA-LACTAMASE''' | + | {{Structure |
| + | |PDB= 1e25 |SIZE=350|CAPTION= <scene name='initialview01'>1e25</scene>, resolution 1.90Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= BLAPER-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 Pseudomonas aeruginosa]) | ||
| + | }} | ||
| + | |||
| + | '''THE HIGH RESOLUTION STRUCTURE OF PER-1 CLASS A BETA-LACTAMASE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1E25 is a [ | + | 1E25 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E25 OCA]. |
==Reference== | ==Reference== | ||
| - | The high resolution crystal structure for class A beta-lactamase PER-1 reveals the bases for its increase in breadth of activity., Tranier S, Bouthors AT, Maveyraud L, Guillet V, Sougakoff W, Samama JP, J Biol Chem. 2000 Sep 8;275(36):28075-82. PMID:[http:// | + | The high resolution crystal structure for class A beta-lactamase PER-1 reveals the bases for its increase in breadth of activity., Tranier S, Bouthors AT, Maveyraud L, Guillet V, Sougakoff W, Samama JP, J Biol Chem. 2000 Sep 8;275(36):28075-82. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10825176 10825176] |
[[Category: Beta-lactamase]] | [[Category: Beta-lactamase]] | ||
[[Category: Pseudomonas aeruginosa]] | [[Category: Pseudomonas aeruginosa]] | ||
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[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:48:16 2008'' |
Revision as of 08:48, 20 March 2008
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| , resolution 1.90Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | BLAPER-1 (Pseudomonas aeruginosa) | ||||||
| Activity: | Beta-lactamase, with EC number 3.5.2.6 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE HIGH RESOLUTION STRUCTURE OF PER-1 CLASS A BETA-LACTAMASE
Overview
The treatment of infectious diseases by beta-lactam antibiotics is continuously challenged by the emergence and dissemination of new beta-lactamases. In most cases, the cephalosporinase activity of class A enzymes results from a few mutations in the TEM and SHV penicillinases. The PER-1 beta-lactamase was characterized as a class A enzyme displaying a cephalosporinase activity. This activity was, however, insensitive to the mutations of residues known to be critical for providing extended substrate profiles to TEM and SHV. The x-ray structure of the protein, solved at 1.9-A resolution, reveals that two of the most conserved features in class A beta-lactamases are not present in this enzyme: the fold of the Omega-loop and the cis conformation of the peptide bond between residues 166 and 167. The new fold of the Omega-loop and the insertion of four residues at the edge of strand S3 generate a broad cavity that may easily accommodate the bulky substituents of cephalosporin substrates. The trans conformation of the 166-167 bond is related to the presence of an aspartic acid at position 136. Selection of class A enzymes based on the occurrence of both Asp(136) and Asn(179) identifies a subgroup of enzymes with high sequence homology.
About this Structure
1E25 is a Single protein structure of sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA.
Reference
The high resolution crystal structure for class A beta-lactamase PER-1 reveals the bases for its increase in breadth of activity., Tranier S, Bouthors AT, Maveyraud L, Guillet V, Sougakoff W, Samama JP, J Biol Chem. 2000 Sep 8;275(36):28075-82. PMID:10825176
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