1e25

<table><tr><td colspan='2'>[[1e25]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E25 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1E25 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BLAPER-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 "Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885])</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1e25 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e25 OCA], [http://pdbe.org/1e25 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1e25 RCSB], [http://www.ebi.ac.uk/pdbsum/1e25 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1e25 ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:10825176</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1e25" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Beta-lactamase]]

[[Category: Bouthors, A T]]

[[Category: Guillet, V]]

[[Category: Maveyraud, L]]

[[Category: Samama, J P]]

[[Category: Sougakoff, W]]

[[Category: Tranier, S]]

[[Category: Hydrolase]]