1e25

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[[Image:1e25.gif|left|200px]]
[[Image:1e25.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1e25 |SIZE=350|CAPTION= <scene name='initialview01'>1e25</scene>, resolution 1.90&Aring;
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The line below this paragraph, containing "STRUCTURE_1e25", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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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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or leave the SCENE parameter empty for the default display.
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|GENE= BLAPER-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 Pseudomonas aeruginosa])
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-->
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|DOMAIN=
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{{STRUCTURE_1e25| PDB=1e25 | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e25 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e25 OCA], [http://www.ebi.ac.uk/pdbsum/1e25 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1e25 RCSB]</span>
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}}
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'''THE HIGH RESOLUTION STRUCTURE OF PER-1 CLASS A BETA-LACTAMASE'''
'''THE HIGH RESOLUTION STRUCTURE OF PER-1 CLASS A BETA-LACTAMASE'''
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[[Category: Sougakoff, W.]]
[[Category: Sougakoff, W.]]
[[Category: Tranier, S.]]
[[Category: Tranier, S.]]
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[[Category: antibiotic resistance]]
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[[Category: Antibiotic resistance]]
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[[Category: class a cephalosporinase]]
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[[Category: Class a cephalosporinase]]
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[[Category: hydrolase]]
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[[Category: Hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:33:53 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:53:30 2008''
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Revision as of 11:33, 2 May 2008

Image:1e25.gif

Template:STRUCTURE 1e25

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 Page seeded by OCA on Fri May 2 14:33:53 2008

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