4csc: Difference between revisions

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-[[Image:4csc.gif|left|200px]]
- {{Structure
+==STRUCTURE OF TERNARY COMPLEXES OF CITRATE SYNTHASE WITH D-AND L-MALATE: MECHANISTIC IMPLICATIONS==
-|PDB= 4csc |SIZE=350|CAPTION= <scene name='initialview01'>4csc</scene>, resolution 1.9&Aring;
+<StructureSection load='4csc' size='340' side='right'caption='[[4csc]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=MAL:MALTOSE'>MAL</scene> and <scene name='pdbligand=ACO:ACETYL COENZYME *A'>ACO</scene>
+<table><tr><td colspan='2'>[[4csc]] 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=4CSC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CSC FirstGlance]. <br>
-|ACTIVITY= [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]
+</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>
-|GENE=
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene>, <scene name='pdbligand=MLT:D-MALATE'>MLT</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=4csc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4csc OCA], [https://pdbe.org/4csc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4csc RCSB], [https://www.ebi.ac.uk/pdbsum/4csc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4csc 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/4csc_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=4csc ConSurf].
+<div style="clear:both"></div>
-'''STRUCTURE OF TERNARY COMPLEXES OF CITRATE SYNTHASE WITH D-AND L-MALATE: MECHANISTIC IMPLICATIONS'''
+==See Also==
+*[[Citrate Synthase 3D structures|Citrate Synthase 3D structures]]
+__TOC__
-==Overview==
+</StructureSection>
-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).
-==About this Structure==
-CSC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CSC OCA].
-==Reference==
-.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://www.ncbi.nlm.nih.gov/pubmed/2043640 2043640]
-[[Category: Citrate (Si)-synthase]]
 [[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: ACO]]
-[[Category: MAL]]
-[[Category: oxo-acid-lyase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 19:09:19 2008''