1ee2: Difference between revisions
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==THE STRUCTURE OF STEROID-ACTIVE ALCOHOL DEHYDROGENASE AT 1.54 A RESOLUTION== | ==THE STRUCTURE OF STEROID-ACTIVE ALCOHOL DEHYDROGENASE AT 1.54 A RESOLUTION== | ||
<StructureSection load='1ee2' size='340' side='right' caption='[[1ee2]], [[Resolution|resolution]] 1.54Å' scene=''> | <StructureSection load='1ee2' size='340' side='right'caption='[[1ee2]], [[Resolution|resolution]] 1.54Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1ee2]] is a 2 chain structure with 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=1EE2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EE2 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1ee2]] is a 2 chain structure with 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=1EE2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EE2 FirstGlance]. <br> | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ee/1ee2_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ee/1ee2_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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==See Also== | ==See Also== | ||
*[[Alcohol dehydrogenase|Alcohol dehydrogenase]] | *[[Alcohol dehydrogenase 3D structures|Alcohol dehydrogenase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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[[Category: Alcohol dehydrogenase]] | [[Category: Alcohol dehydrogenase]] | ||
[[Category: Equus caballus]] | [[Category: Equus caballus]] | ||
[[Category: Large Structures]] | |||
[[Category: Adolph, H W]] | [[Category: Adolph, H W]] | ||
[[Category: Alcohol]] | [[Category: Alcohol]] | ||
Revision as of 09:54, 12 June 2019
THE STRUCTURE OF STEROID-ACTIVE ALCOHOL DEHYDROGENASE AT 1.54 A RESOLUTIONTHE STRUCTURE OF STEROID-ACTIVE ALCOHOL DEHYDROGENASE AT 1.54 A RESOLUTION
Structural highlights
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 PubMedA structure determination in combination with a kinetic study of the steroid converting isozyme of horse liver alcohol dehydrogenase, SS-ADH, is presented. Kinetic parameters for the substrates, 5beta-androstane-3beta,17beta-ol, 5beta-androstane-17beta-ol-3-one, ethanol, and various secondary alcohols and the corresponding ketones are compared for the SS- and EE-isozymes which differ by nine amino acid substitutions and one deletion. Differences in substrate specificity and stereoselectivity are explained on the basis of individual kinetic rate constants for the underlying ordered bi-bi mechanism. SS-ADH was crystallized in complex with 3alpha,7alpha,12alpha-trihydroxy-5beta-cholan -24-acid (cholic acid) and NAD(+), but microspectrophotometric analysis of single crystals proved it to be a mixed complex containing 60-70% NAD(+) and 30-40% NADH. The crystals belong to the space group P2(1) with cell dimensions a = 55.0 A, b = 73.2 A, c = 92.5 A, and beta = 102.5 degrees. A 98% complete data set to 1.54-A resolution was collected at 100 K using synchrotron radiation. The structure was solved by the molecular replacement method utilizing EE-ADH as the search model. The major structural difference between the isozymes is a widening of the substrate channel. The largest shifts in C(alpha) carbon positions (about 5 A) are observed in the loop region, in which a deletion of Asp115 is found in the SS isozyme. SS-ADH easily accommodates cholic acid, whereas steroid substrates of similar bulkiness would not fit into the EE-ADH substrate site. In the ternary complex with NAD(+)/NADH, we find that the carboxyl group of cholic acid ligates to the active site zinc ion, which probably contributes to the strong binding in the ternary NAD(+) complex. Structural basis for substrate specificity differences of horse liver alcohol dehydrogenase isozymes.,Adolph HW, Zwart P, Meijers R, Hubatsch I, Kiefer M, Lamzin V, Cedergren-Zeppezauer E Biochemistry. 2000 Oct 24;39(42):12885-97. PMID:11041853[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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