1adb

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(New page: 200px<br /><applet load="1adb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1adb, resolution 2.4&Aring;" /> '''CRYSTALLOGRAPHIC STUD...)
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[[Image:1adb.gif|left|200px]]<br /><applet load="1adb" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1adb, resolution 2.4&Aring;" />
 
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'''CRYSTALLOGRAPHIC STUDIES OF ISOSTERIC NAD ANALOGUES BOUND TO ALCOHOL DEHYDROGENASE: SPECIFICITY AND SUBSTRATE BINDING IN TWO TERNARY COMPLEXES'''<br />
 
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==Overview==
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==CRYSTALLOGRAPHIC STUDIES OF ISOSTERIC NAD ANALOGUES BOUND TO ALCOHOL DEHYDROGENASE: SPECIFICITY AND SUBSTRATE BINDING IN TWO TERNARY COMPLEXES==
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CNAD (5-beta-D-ribofuranosylnicotinamide adenine dinucleotide) is an, isosteric C-glycosidic analogue of NAD(H) containing a neutral pyridine, ring. CPAD (5-beta-D-ribofuranosylpicolinamide adenine dinucleotide) is a, closely related pyridine-containing analogue with the pyridine nitrogen on, the opposite side of the ring. CNAD is a potent and specific inhibitor of, horse liver alcohol dehydrogenase (LADH), binding with a dissociation, constant in the nanomolar range. CPAD binds LADH with an affinity, comparable to that of NAD. Crystal structures of CNAD and CPAD bound to, LADH are presented at 2.4 and 2.7 A, respectively. The two complexes are, isomorphous, crystallizing in the triclinic system with cell dimensions, different from those seen in previous ternary LADH complexes. Structures, were solved using the molecular replacement method and refined to, crystallographic R values of 18% (CNAD) and 17% (CPAD). Both inhibitors, bind to the "closed" form of LADH in the normal cofactor-binding cleft., The conformation of LADH-bound CPAD closely mimics that of LADH-bound, NAD(H). The data suggest that alcohol substrate binds directly to the, catalytic zinc atom. In the CNAD complex, the pyridine nitrogen replaces, alcohol as the fourth coordination ligand to the active site zinc atom, while all other polar interactions remain the same as those of bound, NAD(H). The zinc-nitrogen ligand explains the high affinity of CNAD for, LADH.
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<StructureSection load='1adb' size='340' side='right'caption='[[1adb]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1adb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ADB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ADB FirstGlance]. <br>
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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]] 2.4&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CND:5-BETA-D-RIBOFURANOSYLNICOTINAMIDE+ADENINE+DINUCLEOTIDE'>CND</scene>, <scene name='pdbligand=EOH:ETHANOL'>EOH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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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=1adb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1adb OCA], [https://pdbe.org/1adb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1adb RCSB], [https://www.ebi.ac.uk/pdbsum/1adb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1adb ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ADH1E_HORSE ADH1E_HORSE]
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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/ad/1adb_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=1adb ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1ADB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus] with ZN, CND and EOH as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Alcohol_dehydrogenase Alcohol dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.1 1.1.1.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ADB OCA].
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*[[Alcohol dehydrogenase 3D structures|Alcohol dehydrogenase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Crystallographic studies of isosteric NAD analogues bound to alcohol dehydrogenase: specificity and substrate binding in two ternary complexes., Li H, Hallows WH, Punzi JS, Pankiewicz KW, Watanabe KA, Goldstein BM, Biochemistry. 1994 Oct 4;33(39):11734-44. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7918390 7918390]
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[[Category: Alcohol dehydrogenase]]
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[[Category: Equus caballus]]
[[Category: Equus caballus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Goldstein, B.M.]]
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[[Category: Goldstein BM]]
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[[Category: Hallows, W.A.]]
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[[Category: Hallows WA]]
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[[Category: Li, H.]]
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[[Category: Li H]]
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[[Category: Pankiewicz, K.W.]]
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[[Category: Pankiewicz KW]]
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[[Category: Punzi, J.S.]]
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[[Category: Punzi JS]]
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[[Category: Watanabe, K.A.]]
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[[Category: Watanabe KA]]
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[[Category: CND]]
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[[Category: EOH]]
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[[Category: ZN]]
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[[Category: oxidoreductase (nad(a)-choh(d))]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:46:11 2007''
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Current revision

CRYSTALLOGRAPHIC STUDIES OF ISOSTERIC NAD ANALOGUES BOUND TO ALCOHOL DEHYDROGENASE: SPECIFICITY AND SUBSTRATE BINDING IN TWO TERNARY COMPLEXES

PDB ID 1adb

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