1ped: Difference between revisions
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==BACTERIAL SECONDARY ALCOHOL DEHYDROGENASE (APO-FORM)== | ==BACTERIAL SECONDARY ALCOHOL DEHYDROGENASE (APO-FORM)== | ||
<StructureSection load='1ped' size='340' side='right' caption='[[1ped]], [[Resolution|resolution]] 2.15Å' scene=''> | <StructureSection load='1ped' size='340' side='right'caption='[[1ped]], [[Resolution|resolution]] 2.15Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1ped]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"clostridium_rubrum"_ng_and_vaughn_1963 "clostridium rubrum" ng and vaughn 1963]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PED OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PED FirstGlance]. <br> | <table><tr><td colspan='2'>[[1ped]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"clostridium_rubrum"_ng_and_vaughn_1963 "clostridium rubrum" ng and vaughn 1963]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PED OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PED FirstGlance]. <br> | ||
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==See Also== | ==See Also== | ||
*[[Alcohol dehydrogenase|Alcohol dehydrogenase]] | |||
*[[Alcohol dehydrogenase 3D structures|Alcohol dehydrogenase 3D structures]] | |||
*[[Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-294 of T. brockii ADH by E. histolytica ADH|Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-294 of T. brockii ADH by E. histolytica ADH]] | *[[Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-294 of T. brockii ADH by E. histolytica ADH|Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-294 of T. brockii ADH by E. histolytica ADH]] | ||
*[[Chimeras of alcohol dehydrogenases|Chimeras of alcohol dehydrogenases]] | *[[Chimeras of alcohol dehydrogenases|Chimeras of alcohol dehydrogenases]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Clostridium rubrum ng and vaughn 1963]] | [[Category: Clostridium rubrum ng and vaughn 1963]] | ||
[[Category: Large Structures]] | |||
[[Category: Frolow, F]] | [[Category: Frolow, F]] | ||
[[Category: Korkhin, Y]] | [[Category: Korkhin, Y]] | ||
Revision as of 12:59, 27 November 2019
BACTERIAL SECONDARY ALCOHOL DEHYDROGENASE (APO-FORM)BACTERIAL SECONDARY ALCOHOL DEHYDROGENASE (APO-FORM)
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 PubMedTwo 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
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