5cts: Difference between revisions

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New page: left|200px<br /><applet load="5cts" size="450" color="white" frame="true" align="right" spinBox="true" caption="5cts, resolution 1.9Å" /> '''PROPOSED MECHANISM FO...
 
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[[Image:5cts.gif|left|200px]]<br /><applet load="5cts" size="450" color="white" frame="true" align="right" spinBox="true"
caption="5cts, resolution 1.9&Aring;" />
'''PROPOSED MECHANISM FOR THE CONDENSATION REACTION OF CITRATE SYNTHASE. 1.9-ANGSTROMS STRUCTURE OF THE TERNARY COMPLEX WITH OXALOACETATE AND CARBOXYMETHYL COENZYME A'''<br />


==Overview==
==PROPOSED MECHANISM FOR THE CONDENSATION REACTION OF CITRATE SYNTHASE. 1.9-ANGSTROMS STRUCTURE OF THE TERNARY COMPLEX WITH OXALOACETATE AND CARBOXYMETHYL COENZYME A==
The crystal structure of the ternary complex citrate, synthase-oxaloacetate-carboxymethyl coenzyme A has been solved to a, resolution of 1.9 A and refined to a conventional crystallographic R, factor of 0.185. The structure resembles a proposed transition state of, the condensation reaction and suggests that the condensation reaction, proceeds through a neutral enol rather than an enolate intermediate. A, mechanism for the condensation reaction is proposed which involves the, participation of three key catalytic groups (Asp 375, His 274, and His, 320) in two distinct steps. The proposed mechanism invokes concerted, general acid-base catalysis twice to explain both the energetics of the, reaction and the experimentally observed inversion of stereochemistry at, the attacking carbon atom.
<StructureSection load='5cts' size='340' side='right'caption='[[5cts]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5cts]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CTS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CTS FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CMC:CARBOXYMETHYL+COENZYME+*A'>CMC</scene>, <scene name='pdbligand=OAA:OXALOACETATE+ION'>OAA</scene></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=5cts FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cts OCA], [https://pdbe.org/5cts PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cts RCSB], [https://www.ebi.ac.uk/pdbsum/5cts PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cts ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CISY_CHICK CISY_CHICK]
== 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/ct/5cts_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=5cts ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
5CTS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with OAA and CMC as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Citrate_(Si)-synthase Citrate (Si)-synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.3.1 2.3.3.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=5CTS OCA].
*[[Citrate Synthase|Citrate Synthase]]
 
*[[Citrate Synthase 3D structures|Citrate Synthase 3D structures]]
==Reference==
__TOC__
Proposed mechanism for the condensation reaction of citrate synthase: 1.9-A structure of the ternary complex with oxaloacetate and carboxymethyl coenzyme A., Karpusas M, Branchaud B, Remington SJ, Biochemistry. 1990 Mar 6;29(9):2213-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=2337600 2337600]
</StructureSection>
[[Category: Citrate (Si)-synthase]]
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Branchaud, B.]]
[[Category: Branchaud B]]
[[Category: Karpusas, M.]]
[[Category: Karpusas M]]
[[Category: Remington, S.J.]]
[[Category: Remington SJ]]
[[Category: CMC]]
[[Category: OAA]]
[[Category: oxo-acid-lyase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:28:07 2007''

Latest revision as of 15:21, 6 March 2024

PROPOSED MECHANISM FOR THE CONDENSATION REACTION OF CITRATE SYNTHASE. 1.9-ANGSTROMS STRUCTURE OF THE TERNARY COMPLEX WITH OXALOACETATE AND CARBOXYMETHYL COENZYME APROPOSED MECHANISM FOR THE CONDENSATION REACTION OF CITRATE SYNTHASE. 1.9-ANGSTROMS STRUCTURE OF THE TERNARY COMPLEX WITH OXALOACETATE AND CARBOXYMETHYL COENZYME A

Structural highlights

5cts is a 1 chain structure with sequence from Gallus gallus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CISY_CHICK

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

5cts, resolution 1.90Å

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