3lez

<StructureSection load='3lez' size='340' side='right' caption='[[3lez]], [[Resolution|resolution]] 1.25&Aring;' scene=''>

<table><tr><td colspan='2'>[[3lez]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Dsm_14371 Dsm 14371]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LEZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LEZ FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">OB2793, oih-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=182710 DSM 14371])</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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3lez FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lez OCA], [http://pdbe.org/3lez PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3lez RCSB], [http://www.ebi.ac.uk/pdbsum/3lez PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3lez ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

We describe herein a highly proficient class A beta-lactamase OIH-1 from the bacterium Oceanobacillus iheyensis, whose habitat is the sediment at a depth of 1050 m in the Pacific Ocean. The OIH-1 structure was solved by molecular replacement and refined at 1.25 A resolution. OIH-1 has evolved to be an extremely halotolerant beta-lactamase capable of hydrolyzing its substrates in the presence of NaCl at saturating concentration. Not only is this the most highly halotolerant bacterial enzyme structure known to date, it is also the highest resolution halophilic protein structure yet determined. Evolution of OIH-1 in the salinity of the ocean has resulted in a molecular surface that is coated with acidic residues, a marked difference from beta-lactamases of terrestrial sources. OIH-1 is the first example of an antibiotic-resistance enzyme that has evolved in the depths of the ocean in isolation from clinical selection and gives us an extraordinary glimpse into protein evolution under extreme conditions. It represents evidence for the existence of a reservoir of antibiotic-resistance enzymes in nature among microbial populations from deep oceanic sources.

An antibiotic-resistance enzyme from a deep-sea bacterium.,Toth M, Smith C, Frase H, Mobashery S, Vakulenko S J Am Chem Soc. 2010 Jan 20;132(2):816-23. PMID:20000704<ref>PMID:20000704</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 3lez" style="background-color:#fffaf0;"></div>

*[[Beta-lactamase|Beta-lactamase]]

[[Category: Beta-lactamase]]

[[Category: Dsm 14371]]

[[Category: Smith, C A]]

[[Category: Vakulenko, S B]]

[[Category: Hydrolase]]