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| | <StructureSection load='1hxh' size='340' side='right'caption='[[1hxh]], [[Resolution|resolution]] 1.22Å' scene=''> | | <StructureSection load='1hxh' size='340' side='right'caption='[[1hxh]], [[Resolution|resolution]] 1.22Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1hxh]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_11996 Atcc 11996]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HXH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HXH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1hxh]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Comamonas_testosteroni Comamonas testosteroni]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HXH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HXH FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2hsd|2hsd]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.22Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></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=1hxh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hxh OCA], [https://pdbe.org/1hxh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hxh RCSB], [https://www.ebi.ac.uk/pdbsum/1hxh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hxh ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hxh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hxh OCA], [http://pdbe.org/1hxh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hxh RCSB], [http://www.ebi.ac.uk/pdbsum/1hxh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1hxh ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/3BHD_COMTE 3BHD_COMTE] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 11996]] | + | [[Category: Comamonas testosteroni]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Benach, J]] | + | [[Category: Benach J]] |
| - | [[Category: Berndt, K D]] | + | [[Category: Berndt KD]] |
| - | [[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 C.T]] | + | [[Category: Oppermann UCT]] |
| - | [[Category: Roversi, P]] | + | [[Category: Roversi P]] |
| - | [[Category: Alpha-beta]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Rossmann fold]]
| + | |
| - | [[Category: Short-chain dehydrogenase]]
| + | |
| Structural highlights
Function
3BHD_COMTE
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
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Benach J, Filling C, Oppermann UC, Roversi P, Bricogne G, Berndt KD, Jornvall H, Ladenstein R. Structure of bacterial 3beta/17beta-hydroxysteroid dehydrogenase at 1.2 A resolution: a model for multiple steroid recognition. Biochemistry. 2002 Dec 17;41(50):14659-68. PMID:12475215
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