1jgt

<table><tr><td colspan='2'>[[1jgt]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/As_4.1611 As 4.1611]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JGT OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1JGT FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=APC:DIPHOSPHOMETHYLPHOSPHONIC+ACID+ADENOSYL+ESTER'>APC</scene>, <scene name='pdbligand=CMA:N2-(CARBOXYETHYL)-L-ARGININE'>CMA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">1901 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1901 AS 4.1611])</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=1jgt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jgt OCA], [http://pdbe.org/1jgt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jgt RCSB], [http://www.ebi.ac.uk/pdbsum/1jgt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1jgt ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

The enzyme beta-lactam synthetase (beta-LS) catalyzes the formation of the beta-lactam ring in clavulanic acid, a clinically important beta-lactamase inhibitor. Whereas the penicillin beta-lactam ring is generated by isopenicillin N synthase (IPNS) in the presence of ferrous ion and dioxygen, beta-LS uses ATP and Mg2+ as cofactors. According to sequence alignments, beta-LS is homologous to class B asparagine synthetases (AS-Bs), ATP/Mg2+-dependent enzymes that convert aspartic acid to asparagine. Here we report the first crystal structure of a beta-LS. The 1.95 A resolution structure of Streptomyces clavuligerus beta-LS provides a fully resolved view of the active site in which substrate, closely related ATP analog alpha,beta-methyleneadenosine 5'-triphosphate (AMP-CPP) and a single Mg2+ ion are present. A high degree of substrate preorganization is observed. Comparison to Escherichia coli AS-B reveals the evolutionary changes that have taken place in beta-LS that impede interdomain reaction, which is essential in AS-B, and that accommodate beta-lactam formation. The structural data provide the opportunity to alter the synthetic potential of beta-LS, perhaps leading to the creation of new beta-lactamase inhibitors and beta-lactam antibiotics.

Structure of beta-lactam synthetase reveals how to synthesize antibiotics instead of asparagine.,Miller MT, Bachmann BO, Townsend CA, Rosenzweig AC Nat Struct Biol. 2001 Aug;8(8):684-9. PMID:11473258<ref>PMID:11473258</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 1jgt" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: As 4 1611]]

[[Category: Bachmann, B O]]

[[Category: Miller, M T]]

[[Category: Rosenzweig, A C]]

[[Category: Townsend, C A]]

[[Category: Ampcpp]]

[[Category: Hydrolase]]