1csc: Difference between revisions

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New page: left|200px<br /><applet load="1csc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1csc, resolution 1.7Å" /> '''STRUCTURE OF TERNARY ...
 
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[[Image:1csc.gif|left|200px]]<br /><applet load="1csc" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1csc, resolution 1.7&Aring;" />
'''STRUCTURE OF TERNARY COMPLEXES OF CITRATE SYNTHASE WITH D-AND L-MALATE: MECHANISTIC IMPLICATIONS'''<br />


==Overview==
==Structure of ternary complexes of citrate synthase with D-and L-malate: Mechanistic implications==
The structures of four isomorphous crystals of ternary complexes of, chicken heart citrate synthase with D- or L-malate and acetyl coenzyme A, or carboxymethyl coenzyme A have been determined by X-ray crystallography, and fully refined at 1.9-A resolution. The structures show that both, L-malate and D-malate bind in a very similar way in the presence of, acetylCoA and that the enzyme conformation is "closed". Hydrogen bond, geometry is suggested to account for the difference in binding constants, of the two stereoisomers. The structures suggest that steric hindrance can, account for the observation that proton exchange of acetyl coenzyme A with, solvent is catalyzed by citrate synthase in the presence of L-malate but, not D-malate. The ternary complexes with malate reveal the mode of binding, of the substrate acetylCoA in the ground state. The carbonyl oxygen of the, acetyl group is hydrogen bonded to a water molecule and to histidine 274, allowing unambiguous identification of the orientation of this group. The, structures support the hypothesis that carboxymethyl coenzyme A is a, transition-state analogue for the enolization step of the reaction (Bayer, et al., 1981) and additionally support proposed mechanisms for the, condensation reaction (Karpusas et al., 1990; Alter et al., 1990).
<StructureSection load='1csc' size='340' side='right'caption='[[1csc]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1csc]] 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=1CSC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CSC 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]] 1.7&#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=LMR:(2S)-2-HYDROXYBUTANEDIOIC+ACID'>LMR</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=1csc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1csc OCA], [https://pdbe.org/1csc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1csc RCSB], [https://www.ebi.ac.uk/pdbsum/1csc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1csc 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/cs/1csc_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=1csc ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1CSC 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 MAL 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=1CSC OCA].
*[[Citrate Synthase 3D structures|Citrate Synthase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
1.9-A structures of ternary complexes of citrate synthase with D- and L-malate: mechanistic implications., Karpusas M, Holland D, Remington SJ, Biochemistry. 1991 Jun 18;30(24):6024-31. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=2043640 2043640]
[[Category: Citrate (Si)-synthase]]
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Holland, D.]]
[[Category: Holland D]]
[[Category: Karpusas, M.]]
[[Category: Karpusas M]]
[[Category: Remington, S.J.]]
[[Category: Remington SJ]]
[[Category: CMC]]
[[Category: MAL]]
[[Category: oxo-acid-lyase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:43:14 2007''

Latest revision as of 09:45, 7 February 2024

Structure of ternary complexes of citrate synthase with D-and L-malate: Mechanistic implicationsStructure of ternary complexes of citrate synthase with D-and L-malate: Mechanistic implications

Structural highlights

1csc 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 1.7Å
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

1csc, resolution 1.70Å

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