1adb: Difference between revisions

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-[[Image:1adb.gif|left|200px]]
- {{Structure
+==CRYSTALLOGRAPHIC STUDIES OF ISOSTERIC NAD ANALOGUES BOUND TO ALCOHOL DEHYDROGENASE: SPECIFICITY AND SUBSTRATE BINDING IN TWO TERNARY COMPLEXES==
-|PDB= 1adb |SIZE=350|CAPTION= <scene name='initialview01'>1adb</scene>, resolution 2.4&Aring;
+<StructureSection load='1adb' size='340' side='right'caption='[[1adb]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <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>
+<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>
-|ACTIVITY= <span class='plainlinks'>[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] </span>
+</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>
-|GENE=
+<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>
-|DOMAIN=
+<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>
-|RELATEDENTRY=
+</table>
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1adb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1adb OCA], [http://www.ebi.ac.uk/pdbsum/1adb PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1adb RCSB]</span>
+== Function ==
-}}
+[https://www.uniprot.org/uniprot/ADH1E_HORSE ADH1E_HORSE]
+== 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/ad/1adb_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=1adb ConSurf].
+<div style="clear:both"></div>
-'''CRYSTALLOGRAPHIC STUDIES OF ISOSTERIC NAD ANALOGUES BOUND TO ALCOHOL DEHYDROGENASE: SPECIFICITY AND SUBSTRATE BINDING IN TWO TERNARY COMPLEXES'''
+==See Also==
+*[[Alcohol dehydrogenase 3D structures|Alcohol dehydrogenase 3D structures]]
+__TOC__
-==Overview==
+</StructureSection>
-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.
-==About this Structure==
-ADB is a [[Single protein]] structure of sequence from [http://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].
-==Reference==
-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://www.ncbi.nlm.nih.gov/pubmed/7918390 7918390]
-[[Category: Alcohol dehydrogenase]]
 [[Category: Equus caballus]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Goldstein, B M.]]
+[[Category: Goldstein BM]]
-[[Category: Hallows, W A.]]
+[[Category: Hallows WA]]
-[[Category: Li, H.]]
+[[Category: Li H]]
-[[Category: Pankiewicz, K W.]]
+[[Category: Pankiewicz KW]]
-[[Category: Punzi, J S.]]
+[[Category: Punzi JS]]
-[[Category: Watanabe, K A.]]
+[[Category: Watanabe KA]]
-[[Category: oxidoreductase (nad(a)-choh(d))]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:37:51 2008''