1csi: Difference between revisions

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<StructureSection load='1csi' size='340' side='right'caption='[[1csi]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='1csi' size='340' side='right'caption='[[1csi]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1csi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Chick Chick]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CSI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CSI FirstGlance]. <br>
<table><tr><td colspan='2'>[[1csi]] 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=1CSI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CSI FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CMX:CARBOXYMETHYLDETHIA+COENZYME+*A'>CMX</scene>, <scene name='pdbligand=OAA:OXALOACETATE+ION'>OAA</scene></td></tr>
</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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Citrate_(Si)-synthase Citrate (Si)-synthase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.3.1 2.3.3.1] </span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CMX:CARBOXYMETHYLDETHIA+COENZYME+*A'>CMX</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=1csi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1csi OCA], [https://pdbe.org/1csi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1csi RCSB], [https://www.ebi.ac.uk/pdbsum/1csi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1csi ProSAT]</span></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=1csi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1csi OCA], [https://pdbe.org/1csi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1csi RCSB], [https://www.ebi.ac.uk/pdbsum/1csi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1csi ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CISY_CHICK CISY_CHICK]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1csi ConSurf].
</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=1csi ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Two extremely potent inhibitors of citrate synthase, carboxyl and primary amide analogues of acetyl coenzyme A, have been synthesized. The ternary complexes of these inhibitors with oxaloacetate and citrate synthase have been crystallized and their structures analyzed at 1.70- and 1.65-A resolution, respectively. The inhibitors have dissociation constants in the nanomolar range, with the carboxyl analogue binding more tightly (Ki = 1.6 nM at pH 6.0) than the amide analogue (28 nM), despite the unfavorable requirement for proton uptake by the former. The carboxyl group forms a shorter hydrogen bond with the catalytic Asp 375 (distance &lt; 2.4 A) than does the amide group (distance approximately 2.5 A). Particularly with the carboxylate inhibitor, the very short hydrogen bond distances measured suggest a low barrier or short strong hydrogen bond. However, the binding constants differ by only a factor of 20 at pH 6.0, corresponding to an increase in binding energy for the carboxyl analogue on the enzyme of about 2 kcal/mol more than the amide analogue, much less than has been proposed for short strong hydrogen bonds based on gas phase measurements [&gt; 20 kcal/mol (Gerlt &amp; Gassman, 1993a,b)]. The inhibitor complexes support proposals that Asp 375 and His 274 work in concert to form an enolized form of acetyl-coenzyme A as the first step in the reaction.
A very short hydrogen bond provides only moderate stabilization of an enzyme-inhibitor complex of citrate synthase.,Usher KC, Remington SJ, Martin DP, Drueckhammer DG Biochemistry. 1994 Jun 28;33(25):7753-9. PMID:8011640<ref>PMID:8011640</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1csi" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Citrate Synthase 3D structures|Citrate Synthase 3D structures]]
*[[Citrate Synthase 3D structures|Citrate Synthase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Chick]]
[[Category: Gallus gallus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Remington, S J]]
[[Category: Remington SJ]]
[[Category: Usher, K C]]
[[Category: Usher KC]]

Latest revision as of 09:45, 7 February 2024

A very short hydrogen bond provides only moderate stabilization of an enzyme: inhibitor complex of citrate synthaseA very short hydrogen bond provides only moderate stabilization of an enzyme: inhibitor complex of citrate synthase

Structural highlights

1csi 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

1csi, resolution 1.70Å

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OCA
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