1hxh: Difference between revisions
New page: left|200px<br /><applet load="1hxh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hxh, resolution 1.22Å" /> '''COMAMONAS TESTOSTERO... |
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[[Image:1hxh.gif|left|200px]]<br /><applet load="1hxh" size=" | [[Image:1hxh.gif|left|200px]]<br /><applet load="1hxh" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1hxh, resolution 1.22Å" /> | caption="1hxh, resolution 1.22Å" /> | ||
'''COMAMONAS TESTOSTERONI 3BETA/17BETA HYDROXYSTEROID DEHYDROGENASE'''<br /> | '''COMAMONAS TESTOSTERONI 3BETA/17BETA HYDROXYSTEROID DEHYDROGENASE'''<br /> | ||
==Overview== | ==Overview== | ||
The enzyme 3beta/17beta-hydroxysteroid dehydrogenase (3beta/17beta-HSD) is | The enzyme 3beta/17beta-hydroxysteroid dehydrogenase (3beta/17beta-HSD) is a steroid-inducible component of the Gram-negative bacterium Comamonas testosteroni. It catalyzes the reversible reduction/dehydrogenation of the oxo/beta-hydroxy groups at positions 3 and 17 of steroid compounds, including hormones and isobile acids. Crystallographic analysis at 1.2 A resolution reveals the enzyme to have nearly identical subunits that form a tetramer with 222 symmetry. This is one of the largest oligomeric structures refined at this resolution. The subunit consists of a monomer with a single-domain structure built around a seven-stranded beta-sheet flanked by six alpha-helices. The active site contains a Ser-Tyr-Lys triad, typical for short-chain dehydrogenases/reductases (SDR). Despite their highly diverse substrate specificities, SDR members show a close to identical folding pattern architectures and a common catalytic mechanism. In contrast to other SDR apostructures determined, the substrate binding loop is well-defined. Analysis of structure-activity relationships of catalytic cleft residues, docking analysis of substrates and inhibitors, and accessible surface analysis explains how 3beta/17beta-HSD accommodates steroid substrates of different conformations. | ||
==About this Structure== | ==About this Structure== | ||
1HXH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Comamonas_testosteroni Comamonas testosteroni]. Active as [http://en.wikipedia.org/wiki/3(or_17)-beta-hydroxysteroid_dehydrogenase 3(or 17)-beta-hydroxysteroid dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.51 1.1.1.51] Full crystallographic information is available from [http:// | 1HXH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Comamonas_testosteroni Comamonas testosteroni]. Active as [http://en.wikipedia.org/wiki/3(or_17)-beta-hydroxysteroid_dehydrogenase 3(or 17)-beta-hydroxysteroid dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.51 1.1.1.51] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HXH OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Benach, J.]] | [[Category: Benach, J.]] | ||
[[Category: Berndt, K | [[Category: Berndt, K D.]] | ||
[[Category: Bricogne, G.]] | [[Category: Bricogne, G.]] | ||
[[Category: Filling, C.]] | [[Category: Filling, C.]] | ||
[[Category: Jornvall, H.]] | [[Category: Jornvall, H.]] | ||
[[Category: Ladenstein, R.]] | [[Category: Ladenstein, R.]] | ||
[[Category: Oppermann, U | [[Category: Oppermann, U C.T.]] | ||
[[Category: Roversi, P.]] | [[Category: Roversi, P.]] | ||
[[Category: alpha-beta]] | [[Category: alpha-beta]] | ||
| Line 26: | Line 26: | ||
[[Category: short-chain dehydrogenase]] | [[Category: short-chain dehydrogenase]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:05:50 2008'' | ||
Revision as of 14:05, 21 February 2008
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COMAMONAS TESTOSTERONI 3BETA/17BETA HYDROXYSTEROID DEHYDROGENASE
OverviewOverview
The enzyme 3beta/17beta-hydroxysteroid dehydrogenase (3beta/17beta-HSD) is a steroid-inducible component of the Gram-negative bacterium Comamonas testosteroni. It catalyzes the reversible reduction/dehydrogenation of the oxo/beta-hydroxy groups at positions 3 and 17 of steroid compounds, including hormones and isobile acids. Crystallographic analysis at 1.2 A resolution reveals the enzyme to have nearly identical subunits that form a tetramer with 222 symmetry. This is one of the largest oligomeric structures refined at this resolution. The subunit consists of a monomer with a single-domain structure built around a seven-stranded beta-sheet flanked by six alpha-helices. The active site contains a Ser-Tyr-Lys triad, typical for short-chain dehydrogenases/reductases (SDR). Despite their highly diverse substrate specificities, SDR members show a close to identical folding pattern architectures and a common catalytic mechanism. In contrast to other SDR apostructures determined, the substrate binding loop is well-defined. Analysis of structure-activity relationships of catalytic cleft residues, docking analysis of substrates and inhibitors, and accessible surface analysis explains how 3beta/17beta-HSD accommodates steroid substrates of different conformations.
About this StructureAbout this Structure
1HXH is a Single protein structure of sequence from Comamonas testosteroni. Active as 3(or 17)-beta-hydroxysteroid dehydrogenase, with EC number 1.1.1.51 Full crystallographic information is available from OCA.
ReferenceReference
Structure of bacterial 3beta/17beta-hydroxysteroid dehydrogenase at 1.2 A resolution: a model for multiple steroid recognition., Benach J, Filling C, Oppermann UC, Roversi P, Bricogne G, Berndt KD, Jornvall H, Ladenstein R, Biochemistry. 2002 Dec 17;41(50):14659-68. PMID:12475215
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