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- | [[Image:1kev.gif|left|200px]]<br /><applet load="1kev" size="450" color="white" frame="true" align="right" spinBox="true" | |
- | caption="1kev, resolution 2.05Å" /> | |
- | '''STRUCTURE OF NADP-DEPENDENT ALCOHOL DEHYDROGENASE'''<br /> | |
| | | |
- | ==Overview== | + | ==STRUCTURE OF NADP-DEPENDENT ALCOHOL DEHYDROGENASE== |
- | Two tetrameric NADP(+)-dependent bacterial secondary alcohol, dehydrogenases have been crystallized in the apo- and the holo-enzyme, forms. Crystals of the holo-enzyme from the mesophilic Clostridium, beijerinckii (NCBAD) belong to space group P2(1)2(1)2(1) with unit-cell, dimensions a = 90.5, b = 127.9, c = 151.4 A. Crystals of the apo-enzyme, (CBAD) belong to the same space group with unit-cell dimensions a = 80.4, b = 102.3, c = 193.5 A. Crystals of the holo-enzyme from the thermophilic, Thermoanaerobium brockii (NTBAD) belong to space group P6(1(5)) (a = b =, 80.6, c = 400.7 A). Crystals of the apo-form of TBAD (point mutant GI98D), belong to space group P2(1) with cell dimensions a = 123.0, b = 84.8, c =, 160.4 A beta = 99.5 degrees. Crystals of CBAD, NCBAD and NTBAD contain one, tetramer per asymmetric unit. They diffract to 2.0 A resolution at liquid, nitrogen temperature. Crystals of TBAD(GI98D) have two tetramers per, asymmetric unit and diffract to 2.7 A at 276 K. Self-rotation analysis, shows that both enzymes are tetramers of 222 symmetry. | + | <StructureSection load='1kev' size='340' side='right'caption='[[1kev]], [[Resolution|resolution]] 2.05Å' scene=''> |
| + | == Structural highlights == |
| + | <table><tr><td colspan='2'>[[1kev]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_beijerinckii Clostridium beijerinckii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KEV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KEV 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]] 2.05Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=1kev FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kev OCA], [https://pdbe.org/1kev PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kev RCSB], [https://www.ebi.ac.uk/pdbsum/1kev PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kev ProSAT]</span></td></tr> |
| + | </table> |
| + | == Function == |
| + | [https://www.uniprot.org/uniprot/ADH_CLOBE ADH_CLOBE] Alcohol dehydrogenase with a preference for medium chain secondary alcohols, such as 2-butanol and isopropanol. Has very low activity with primary alcohols, such as ethanol. Under physiological conditions, the enzyme reduces aldehydes and 2-ketones to produce secondary alcohols. Is active with acetaldehyde and propionaldehyde.<ref>PMID:8349550</ref> <ref>PMID:20102159</ref> |
| + | == 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/ke/1kev_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=1kev ConSurf]. |
| + | <div style="clear:both"></div> |
| + | <div style="background-color:#fffaf0;"> |
| + | == Publication Abstract from PubMed == |
| + | Two tetrameric NADP(+)-dependent bacterial secondary alcohol dehydrogenases have been crystallized in the apo- and the holo-enzyme forms. Crystals of the holo-enzyme from the mesophilic Clostridium beijerinckii (NCBAD) belong to space group P2(1)2(1)2(1) with unit-cell dimensions a = 90.5, b = 127.9, c = 151.4 A. Crystals of the apo-enzyme (CBAD) belong to the same space group with unit-cell dimensions a = 80.4, b = 102.3, c = 193.5 A. Crystals of the holo-enzyme from the thermophilic Thermoanaerobium brockii (NTBAD) belong to space group P6(1(5)) (a = b = 80.6, c = 400.7 A). Crystals of the apo-form of TBAD (point mutant GI98D) belong to space group P2(1) with cell dimensions a = 123.0, b = 84.8, c = 160.4 A beta = 99.5 degrees. Crystals of CBAD, NCBAD and NTBAD contain one tetramer per asymmetric unit. They diffract to 2.0 A resolution at liquid nitrogen temperature. Crystals of TBAD(GI98D) have two tetramers per asymmetric unit and diffract to 2.7 A at 276 K. Self-rotation analysis shows that both enzymes are tetramers of 222 symmetry. |
| | | |
- | ==About this Structure==
| + | Crystalline alcohol dehydrogenases from the mesophilic bacterium Clostridium beijerinckii and the thermophilic bacterium Thermoanaerobium brockii: preparation, characterization and molecular symmetry.,Korkhin Y, Frolow F, Bogin O, Peretz M, Kalb AJ, Burstein Y Acta Crystallogr D Biol Crystallogr. 1996 Jul 1;52(Pt 4):882-6. PMID:15299659<ref>PMID:15299659</ref> |
- | 1KEV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_beijerinckii Clostridium beijerinckii] with ZN and NDP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Alcohol_dehydrogenase_(NADP(+)) Alcohol dehydrogenase (NADP(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.2 1.1.1.2] Known structural/functional Sites: <scene name='pdbsite=S1:Catalytic Site'>S1</scene>, <scene name='pdbsite=S2:Catalytic Site'>S2</scene>, <scene name='pdbsite=S3:Catalytic Site'>S3</scene> and <scene name='pdbsite=S4:Catalytic Site'>S4</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KEV OCA].
| + | |
| | | |
- | ==Reference==
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
- | Crystalline alcohol dehydrogenases from the mesophilic bacterium Clostridium beijerinckii and the thermophilic bacterium Thermoanaerobium brockii: preparation, characterization and molecular symmetry., Korkhin Y, Frolow F, Bogin O, Peretz M, Kalb AJ, Burstein Y, Acta Crystallogr D Biol Crystallogr. 1996 Jul 1;52(Pt 4):882-6. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15299659 15299659]
| + | </div> |
- | [[Category: Alcohol dehydrogenase (NADP(+))]]
| + | <div class="pdbe-citations 1kev" style="background-color:#fffaf0;"></div> |
- | [[Category: Clostridium beijerinckii]]
| + | |
- | [[Category: Single protein]]
| + | |
- | [[Category: Frolow, F.]]
| + | |
- | [[Category: Korkhin, Y.]]
| + | |
- | [[Category: NDP]]
| + | |
- | [[Category: ZN]]
| + | |
- | [[Category: nadp]]
| + | |
- | [[Category: oxidoreductase]]
| + | |
- | [[Category: zinc]]
| + | |
| | | |
- | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 16:41:01 2007''
| + | ==See Also== |
| + | *[[Alcohol dehydrogenase 3D structures|Alcohol dehydrogenase 3D structures]] |
| + | == References == |
| + | <references/> |
| + | __TOC__ |
| + | </StructureSection> |
| + | [[Category: Clostridium beijerinckii]] |
| + | [[Category: Large Structures]] |
| + | [[Category: Frolow F]] |
| + | [[Category: Korkhin Y]] |
| Structural highlights
Function
ADH_CLOBE Alcohol dehydrogenase with a preference for medium chain secondary alcohols, such as 2-butanol and isopropanol. Has very low activity with primary alcohols, such as ethanol. Under physiological conditions, the enzyme reduces aldehydes and 2-ketones to produce secondary alcohols. Is active with acetaldehyde and propionaldehyde.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Two tetrameric NADP(+)-dependent bacterial secondary alcohol dehydrogenases have been crystallized in the apo- and the holo-enzyme forms. Crystals of the holo-enzyme from the mesophilic Clostridium beijerinckii (NCBAD) belong to space group P2(1)2(1)2(1) with unit-cell dimensions a = 90.5, b = 127.9, c = 151.4 A. Crystals of the apo-enzyme (CBAD) belong to the same space group with unit-cell dimensions a = 80.4, b = 102.3, c = 193.5 A. Crystals of the holo-enzyme from the thermophilic Thermoanaerobium brockii (NTBAD) belong to space group P6(1(5)) (a = b = 80.6, c = 400.7 A). Crystals of the apo-form of TBAD (point mutant GI98D) belong to space group P2(1) with cell dimensions a = 123.0, b = 84.8, c = 160.4 A beta = 99.5 degrees. Crystals of CBAD, NCBAD and NTBAD contain one tetramer per asymmetric unit. They diffract to 2.0 A resolution at liquid nitrogen temperature. Crystals of TBAD(GI98D) have two tetramers per asymmetric unit and diffract to 2.7 A at 276 K. Self-rotation analysis shows that both enzymes are tetramers of 222 symmetry.
Crystalline alcohol dehydrogenases from the mesophilic bacterium Clostridium beijerinckii and the thermophilic bacterium Thermoanaerobium brockii: preparation, characterization and molecular symmetry.,Korkhin Y, Frolow F, Bogin O, Peretz M, Kalb AJ, Burstein Y Acta Crystallogr D Biol Crystallogr. 1996 Jul 1;52(Pt 4):882-6. PMID:15299659[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ismaiel AA, Zhu CX, Colby GD, Chen JS. Purification and characterization of a primary-secondary alcohol dehydrogenase from two strains of Clostridium beijerinckii. J Bacteriol. 1993 Aug;175(16):5097-105. PMID:8349550
- ↑ Goihberg E, Peretz M, Tel-Or S, Dym O, Shimon L, Frolow F, Burstein Y. Biochemical and Structural Properties of Chimeras Constructed by Exchange of Cofactor-Binding Domains in Alcohol Dehydrogenases from Thermophilic and Mesophilic Microorganisms. Biochemistry. 2010 Feb 9. PMID:20102159 doi:10.1021/bi901730x
- ↑ Korkhin Y, Frolow F, Bogin O, Peretz M, Kalb AJ, Burstein Y. Crystalline alcohol dehydrogenases from the mesophilic bacterium Clostridium beijerinckii and the thermophilic bacterium Thermoanaerobium brockii: preparation, characterization and molecular symmetry. Acta Crystallogr D Biol Crystallogr. 1996 Jul 1;52(Pt 4):882-6. PMID:15299659 doi:http://dx.doi.org/10.1107/S0907444996001461
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