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New page: left|200px<br /><applet load="1q15" size="450" color="white" frame="true" align="right" spinBox="true" caption="1q15, resolution 2.30Å" /> '''Carbapenam Synthetas...
 
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[[Image:1q15.gif|left|200px]]<br /><applet load="1q15" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1q15, resolution 2.30&Aring;" />
'''Carbapenam Synthetase'''<br />


==Overview==
==Carbapenam Synthetase==
Carbapenam synthetase (CarA) is an ATP/Mg2+-dependent enzyme that, catalyzes formation of the beta-lactam ring in, (5R)-carbapenem-3-carboxylic acid biosynthesis. CarA is homologous to, beta-lactam synthetase (beta-LS), which is involved in clavulanic acid, biosynthesis. The catalytic cycles of CarA and beta-LS mediate substrate, adenylation followed by beta-lactamization via a tetrahedral intermediate, or transition state. Another member of this family of ATP/Mg2+-dependent, enzymes, asparagine synthetase (AS-B), catalyzes intermolecular, rather, than intramolecular, amide bond formation in asparagine biosynthesis. The, crystal structures of apo-CarA and CarA complexed with the substrate, (2S,5S)-5-carboxymethylproline (CMPr), ATP analog, alpha,beta-methyleneadenosine 5'-triphosphate (AMP-CPP), and a single Mg2+, ion have been determined. CarA forms a tetramer. Each monomer resembles, beta-LS and AS-B in overall fold, but key differences are observed. The, N-terminal domain lacks the glutaminase active site found in AS-B, and an, extended loop region not observed in beta-LS or AS-B is present., Comparison of the C-terminal synthetase active site to that in beta-LS, reveals that the ATP binding site is highly conserved. By contrast, variations in the substrate binding pocket reflect the different, substrates of the two enzymes. The Mg2+ coordination is also different., Several key residues in the active site are conserved between CarA and, beta-LS, supporting proposed roles in beta-lactam formation. These data, provide further insight into the structures of this class of enzymes and, suggest that CarA might be a versatile target for protein engineering, experiments aimed at developing improved production methods and new, carbapenem antibiotics.
<StructureSection load='1q15' size='340' side='right'caption='[[1q15]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1q15]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pectobacterium_carotovorum Pectobacterium carotovorum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q15 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Q15 FirstGlance]. <br>
1Q15 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pectobacterium_carotovorum Pectobacterium carotovorum]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Q15 OCA].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
 
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1q15 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q15 OCA], [https://pdbe.org/1q15 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1q15 RCSB], [https://www.ebi.ac.uk/pdbsum/1q15 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1q15 ProSAT]</span></td></tr>
==Reference==
</table>
Crystal structure of carbapenam synthetase (CarA)., Miller MT, Gerratana B, Stapon A, Townsend CA, Rosenzweig AC, J Biol Chem. 2003 Oct 17;278(42):40996-1002. Epub 2003 Jul 30. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12890666 12890666]
== Function ==
[https://www.uniprot.org/uniprot/CARA_PECCC CARA_PECCC] Involved in the biosynthesis of carbapenam-3-carboxylate, a beta-lactam antibiotic of the carbapenem class. Catalyzes the ATP-dependent formation of (3S,5S)-carbapenam-3-carboxylate from (2S,5S)-5-carboxymethylproline.<ref>PMID:12820893</ref> <ref>PMID:17658887</ref> <ref>PMID:19371088</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/q1/1q15_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1q15 ConSurf].
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pectobacterium carotovorum]]
[[Category: Pectobacterium carotovorum]]
[[Category: Single protein]]
[[Category: Gerratana B]]
[[Category: Gerratana, B.]]
[[Category: Miller MT]]
[[Category: Miller, M.T.]]
[[Category: Rosenzweig AC]]
[[Category: Rosenzweig, A.C.]]
[[Category: Stapon A]]
[[Category: Stapon, A.]]
[[Category: Townsend CA]]
[[Category: Townsend, C.A.]]
[[Category: (2s]]
[[Category: 5s)-5-carboxymethylproline; b-ls]]
[[Category: a]]
[[Category: b-lactam synthetase; as-b]]
[[Category: b-methyleneadenosine 5-triphosphate; cea]]
[[Category: class b asparagine synthetase; amp-cpp]]
[[Category: cmpr]]
[[Category: n2-(carboxyethyl)-l-arginine; cma]]
[[Category: n2-(carboxylmethyl)-l-arginine]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 03:22:58 2007''

Latest revision as of 08:12, 14 February 2024

Carbapenam Synthetase

1q15, resolution 2.30Å

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