1css: Difference between revisions

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New page: left|200px<br /><applet load="1css" size="450" color="white" frame="true" align="right" spinBox="true" caption="1css, resolution 1.70Å" /> '''ALPHA-FLUORO ACID AN...
 
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'''ALPHA-FLUORO ACID AND ALPHA-FLUORO AMIDE ANALOGS OF ACETYL-COA AS INHIBITORS OF OF CITRATE SYNTHASE: EFFECT OF PKA MATCHING ON BINDING AFFINITY AND HYDROGEN BOND LENGTH'''<br />


==Overview==
==ALPHA-FLUORO ACID AND ALPHA-FLUORO AMIDE ANALOGS OF ACETYL-COA AS INHIBITORS OF OF CITRATE SYNTHASE: EFFECT OF PKA MATCHING ON BINDING AFFINITY AND HYDROGEN BOND LENGTH==
An alpha-fluoro acid analog and an alpha-fluoro amide analog of acetyl-CoA, have been synthesized. The ternary complexes of these inhibitors with, oxaloacetate and citrate synthase have been crystallized and their, structures analyzed at 1.7 A resolution. The structures are similar to, those reported for the corresponding non-fluorinated analogs (Usher et, al., 1994), with all forming unusually short hydrogen bonds to Asp 375., The alpha-fluoro amide analog binds with an affinity 1.5-fold lower than, that of a previously described amide analog lacking the alpha-fluoro, group. The alpha-fluoro acid analog binds with a 50-fold decreased, affinity relative to the corresponding unfluorinated analog. The binding, affinities are consistent with increased strengths of hydrogen bonds to, Asp 375 with closer matching of pKa values between hydrogen bond donors, and acceptors. The results do not support any direct correlation between, hydrogen bond strength and hydrogen bond length in enzyme-inhibitor, complexes.
<StructureSection load='1css' size='340' side='right'caption='[[1css]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1css]] 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=1CSS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CSS 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=FCX:ALPHA-FLUORO-CARBOXYMETHYLDETHIA+COENZYME+A+COMPLEX'>FCX</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=1css FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1css OCA], [https://pdbe.org/1css PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1css RCSB], [https://www.ebi.ac.uk/pdbsum/1css PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1css 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/1css_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=1css ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1CSS 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 FCX 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=1CSS OCA].
*[[Citrate Synthase 3D structures|Citrate Synthase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
alpha-Fluoro acid and alpha-fluoro amide analogs of acetyl-CoA as inhibitors of citrate synthase: effect of pKa matching on binding affinity and hydrogen bond length., Schwartz B, Drueckhammer DG, Usher KC, Remington SJ, Biochemistry. 1995 Nov 28;34(47):15459-66. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7492547 7492547]
[[Category: Citrate (Si)-synthase]]
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Remington, S.J.]]
[[Category: Remington SJ]]
[[Category: Usher, K.C.]]
[[Category: Usher KC]]
[[Category: FCX]]
[[Category: OAA]]
[[Category: oxo-acid-lyase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:43:58 2007''

Latest revision as of 09:45, 7 February 2024

ALPHA-FLUORO ACID AND ALPHA-FLUORO AMIDE ANALOGS OF ACETYL-COA AS INHIBITORS OF OF CITRATE SYNTHASE: EFFECT OF PKA MATCHING ON BINDING AFFINITY AND HYDROGEN BOND LENGTHALPHA-FLUORO ACID AND ALPHA-FLUORO AMIDE ANALOGS OF ACETYL-COA AS INHIBITORS OF OF CITRATE SYNTHASE: EFFECT OF PKA MATCHING ON BINDING AFFINITY AND HYDROGEN BOND LENGTH

Structural highlights

1css 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

1css, resolution 1.70Å

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