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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>
1JGT 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: 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]]
 
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Retrieved from "https://proteopedia.org/1jgt"