1isk

Revision as of 17:58, 29 October 2007 by OCA (talk | contribs) (New page: left|200px<br /> <applet load="1isk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1isk" /> '''3-OXO-DELTA5-STEROID ISOMERASE, NMR, 20 STR...)
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3-OXO-DELTA5-STEROID ISOMERASE, NMR, 20 STRUCTURES

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1isk

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OverviewOverview

The three-dimensional structure of the enzyme 3-oxo-delta5-steroid, isomerase (E.C. 5.3.3.1), a 28-kilodalton symmetrical dimer, was solved by, multidimensional heteronuclear magnetic resonance spectroscopy. The two, independently folded monomers pack together by means of extensive, hydrophobic and electrostatic interactions. Each monomer comprises three, alpha helices and a six-strand mixed beta-pleated sheet arranged to form a, deep hydrophobic cavity. Catalytically important residues Tyr14 (general, acid) and Asp38 (general base) are located near the bottom of the cavity, and positioned as expected from mechanistic hypotheses. An unexpected acid, group (Asp99) is also located in the active site adjacent to Tyr14, and, kinetic and binding studies of the Asp99 to Ala mutant demonstrate ... [(full description)]

About this StructureAbout this Structure

1ISK is a [Single protein] structure of sequence from [Comamonas testosteroni]. Active as [[1]], with EC number [5.3.3.1]. Full crystallographic information is available from [OCA].

ReferenceReference

Solution structure of 3-oxo-delta5-steroid isomerase., Wu ZR, Ebrahimian S, Zawrotny ME, Thornburg LD, Perez-Alvarado GC, Brothers P, Pollack RM, Summers MF, Science. 1997 Apr 18;276(5311):415-8. PMID:9103200

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