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1jgt

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CRYSTAL STRUCTURE OF BETA-LACTAM SYNTHETASE

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Retrieved from "http://52.214.119.220/wiki/index.php/1jgt"

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-[[Image:1jgt.gif|left|200px]]
- {{Structure
+==CRYSTAL STRUCTURE OF BETA-LACTAM SYNTHETASE==
-|PDB= 1jgt |SIZE=350|CAPTION= <scene name='initialview01'>1jgt</scene>, resolution 1.95&Aring;
+<StructureSection load='1jgt' size='340' side='right'caption='[[1jgt]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <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>
+<table><tr><td colspan='2'>[[1jgt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_clavuligerus Streptomyces clavuligerus]. 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 [https://proteopedia.org/fgij/fg.htm?mol=1JGT FirstGlance]. <br>
-|ACTIVITY=
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95&#8491;</td></tr>
-|GENE= 1901 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1901 Streptomyces clavuligerus])
+<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>
-|DOMAIN=
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1jgt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jgt OCA], [https://pdbe.org/1jgt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jgt RCSB], [https://www.ebi.ac.uk/pdbsum/1jgt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jgt ProSAT]</span></td></tr>
-|RELATEDENTRY=
+</table>
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jgt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jgt OCA], [http://www.ebi.ac.uk/pdbsum/1jgt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jgt RCSB]</span>
+== Function ==
-}}
+[https://www.uniprot.org/uniprot/BLS_STRCL BLS_STRCL]
+== Evolutionary Conservation ==
-'''CRYSTAL STRUCTURE OF BETA-LACTAM SYNTHETASE'''
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
-==Overview==
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jg/1jgt_consurf.spt"</scriptWhenChecked>
-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.
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
-==About this Structure==
+  </jmolCheckbox>
-JGT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_clavuligerus Streptomyces clavuligerus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JGT OCA].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1jgt ConSurf].
+<div style="clear:both"></div>
-==Reference==
+__TOC__
-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:[http://www.ncbi.nlm.nih.gov/pubmed/11473258 11473258]
+</StructureSection>
-[[Category: Single protein]]
+[[Category: Large Structures]]
 [[Category: Streptomyces clavuligerus]]
-[[Category: Bachmann, B O.]]
+[[Category: Bachmann BO]]
-[[Category: Miller, M T.]]
+[[Category: Miller MT]]
-[[Category: Rosenzweig, A C.]]
+[[Category: Rosenzweig AC]]
-[[Category: Townsend, C A.]]
+[[Category: Townsend CA]]
-[[Category: ampcpp]]
-[[Category: asparagine synthetase]]
-[[Category: beta-lactam synthetase]]
-[[Category: carboxyethylarginine]]
-[[Category: cea]]
-[[Category: clavulanic acid]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:33:25 2008''

1jgt

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CRYSTAL STRUCTURE OF BETA-LACTAM SYNTHETASE

Structural highlights

Function

Evolutionary Conservation

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