1ctt

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[[Image:1ctt.gif|left|200px]]
 
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{{Structure
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==TRANSITION-STATE SELECTIVITY FOR A SINGLE OH GROUP DURING CATALYSIS BY CYTIDINE DEAMINASE==
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|PDB= 1ctt |SIZE=350|CAPTION= <scene name='initialview01'>1ctt</scene>, resolution 2.2&Aring;
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<StructureSection load='1ctt' size='340' side='right'caption='[[1ctt]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=DHZ:3,4-DIHYDRO-1H-PYRIMIDIN-2-ONE NUCLEOSIDE'>DHZ</scene>
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<table><tr><td colspan='2'>[[1ctt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CTT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CTT FirstGlance]. <br>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Cytidine_deaminase Cytidine deaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.4.5 3.5.4.5]
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DHZ:3,4-DIHYDRO-1H-PYRIMIDIN-2-ONE+NUCLEOSIDE'>DHZ</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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}}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ctt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ctt OCA], [https://pdbe.org/1ctt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ctt RCSB], [https://www.ebi.ac.uk/pdbsum/1ctt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ctt ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CDD_ECOLI CDD_ECOLI] This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ct/1ctt_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1ctt ConSurf].
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<div style="clear:both"></div>
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'''TRANSITION-STATE SELECTIVITY FOR A SINGLE OH GROUP DURING CATALYSIS BY CYTIDINE DEAMINASE'''
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==See Also==
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*[[Deaminase 3D structures|Deaminase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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Cytidine deaminase binds transition-state analog inhibitors approximately 10(7) times more tightly than corresponding 3,4-dihydro analogs containing a proton in place of the 4-hydroxyl group. X-ray crystal structures of complexes with the two matched inhibitors differ only near a "trapped" water molecule in the complex with the 3,4-dihydro analog, where contacts are substantially less favorable than those with the hydroxyl group of the transition-state analog. The hydrogen bond between the hydroxyl group and the Glu 104 carboxylate shortens in that complex, and may become a "low-barrier" hydrogen bond, since at the same time the bond between zinc and the Cys 132 thiolate ligand lengthens. These differences must therefore account for most of the differential binding affinity related to catalysis. Moreover, the trapped water molecule retains some of the binding energy stabilizing the hydroxyl group in the transition-state analog complex. To this extent, the ratio of binding affinities for the two compounds is smaller than the true contribution of the hydroxyl group, a conclusion with significant bearing on interpreting difference free energies derived from substituent effects arising from chemical modification and/or mutagenesis.
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==About this Structure==
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1CTT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CTT OCA].
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==Reference==
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Transition-state selectivity for a single hydroxyl group during catalysis by cytidine deaminase., Xiang S, Short SA, Wolfenden R, Carter CW Jr, Biochemistry. 1995 Apr 11;34(14):4516-23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7718553 7718553]
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[[Category: Cytidine deaminase]]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Carter, C W.]]
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[[Category: Carter CW]]
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[[Category: Short, S A.]]
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[[Category: Short SA]]
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[[Category: Wolfenden, R.]]
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[[Category: Wolfenden R]]
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[[Category: Xiang, S.]]
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[[Category: Xiang S]]
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[[Category: DHZ]]
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[[Category: ZN]]
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[[Category: hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:28:48 2008''
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Current revision

TRANSITION-STATE SELECTIVITY FOR A SINGLE OH GROUP DURING CATALYSIS BY CYTIDINE DEAMINASE

PDB ID 1ctt

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