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== | ==3-OXO-DELTA5-STEROID ISOMERASE, NMR, 20 STRUCTURES== | ||
The three-dimensional structure of the enzyme 3-oxo-delta5-steroid | <StructureSection load='1isk' size='340' side='right'caption='[[1isk]]' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1isk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Comamonas_testosteroni Comamonas testosteroni]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ISK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ISK FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1isk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1isk OCA], [https://pdbe.org/1isk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1isk RCSB], [https://www.ebi.ac.uk/pdbsum/1isk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1isk ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/SDIS_COMTE SDIS_COMTE] | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/is/1isk_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1isk ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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 that Asp99 contributes to catalysis by stabilizing the intermediate. | |||
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<ref>PMID:9103200</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1isk" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Ketosteroid Isomerase|Ketosteroid Isomerase]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Comamonas testosteroni]] | [[Category: Comamonas testosteroni]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Brothers P]] | |||
[[Category: Brothers | [[Category: Ebrahimian S]] | ||
[[Category: Ebrahimian | [[Category: Perez-Alvarado GC]] | ||
[[Category: Perez-Alvarado | [[Category: Pollack RM]] | ||
[[Category: Pollack | [[Category: Summers MF]] | ||
[[Category: Summers | [[Category: Thornburg LD]] | ||
[[Category: Thornburg | [[Category: Wu ZR]] | ||
[[Category: Wu | [[Category: Zawrotny ME]] | ||
[[Category: Zawrotny | |||
Latest revision as of 11:35, 22 May 2024
3-OXO-DELTA5-STEROID ISOMERASE, NMR, 20 STRUCTURES3-OXO-DELTA5-STEROID ISOMERASE, NMR, 20 STRUCTURES
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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 that Asp99 contributes to catalysis by stabilizing the intermediate. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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