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1w6y

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Revision as of 07:09, 4 April 2018

crystal structure of a mutant W92A in ketosteroid isomerase (KSI) from Pseudomonas putida biotype B

Structural highlights

1w6y is a 1 chain structure with sequence from "bacillus_fluorescens_putidus"_flugge_1886 "bacillus fluorescens putidus" flugge 1886. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	1c7h, 1cqs, 1dmm, 1dmn, 1dmq, 1e3r, 1e3v, 1e97, 1ea2, 1gs3, 1k41, 1ogx, 1oh0, 1oho, 1opy, 1vzz, 1w00, 1w01, 1w02
Activity:	Steroid Delta-isomerase, with EC number 5.3.3.1
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

A structural motif called the small exterior hydrophobic cluster (SEHC) has been proposed to explain the stabilizing effect mediated by solvent-exposed hydrophobic residues; however, little is known about its biological roles. Unusually, in Delta(5)-3-ketosteroid isomerase from Pseudomonas putida biotype B (KSI-PI) Trp92 is exposed to solvent on the protein surface, forming a SEHC with the side-chains of Leu125 and Val127. In order to identify the role of the SEHC in KSI-PI, mutants of those amino acids associated with the SEHC were prepared. The W92A, L125A/V127A, and W92A/L125A/V127A mutations largely decreased the conformational stability, while the L125F/V127F mutation slightly increased the stability, indicating that hydrophobic packing by the SEHC is important in maintaining stability. The crystal structure of W92A revealed that the decreased stability caused by the removal of the bulky side-chain of Trp92 could be attributed to the destabilization of the surface hydrophobic layer consisting of a solvent-exposed beta-sheet. Consistent with the structural data, the binding affinities for three different steroids showed that the surface hydrophobic layer stabilized by SEHC is required for KSI-PI to efficiently recognize hydrophobic steroids. Unfolding kinetics based on analysis of the Phi(U) value also indicated that the SEHC in the native state was resistant to the unfolding process, despite its solvent-exposed site. Taken together, our results demonstrate that the SEHC plays a key role in the structural integrity that is needed for KSI-PI to stabilize the hydrophobic surface conformation and thereby contributes both to the overall conformational stability and to the binding of hydrophobic steroids in water solution.

Small exterior hydrophobic cluster contributes to conformational stability and steroid binding in ketosteroid isomerase from Pseudomonas putida biotype B.,Yun YS, Nam GH, Kim YG, Oh BH, Choi KY FEBS J. 2005 Apr;272(8):1999-2011. PMID:15819891^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Yun YS, Nam GH, Kim YG, Oh BH, Choi KY. Small exterior hydrophobic cluster contributes to conformational stability and steroid binding in ketosteroid isomerase from Pseudomonas putida biotype B. FEBS J. 2005 Apr;272(8):1999-2011. PMID:15819891 doi:10.1111/j.1742-4658.2005.04627.x

1 Structural highlights
2 Evolutionary Conservation
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1w6y"

@@ Line 1: / Line 1: @@
-==CRYSTAL STRUCTURE OF A MUTANT W92A IN KETOSTEROID ISOMERASE (KSI) FROM PSEUDOMONAS PUTIDA BIOTYPE B==
+==crystal structure of a mutant W92A in ketosteroid isomerase (KSI) from Pseudomonas putida biotype B==
 <StructureSection load='1w6y' size='340' side='right' caption='[[1w6y]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 == Structural highlights ==
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1c7h|1c7h]], [[1cqs|1cqs]], [[1dmm|1dmm]], [[1dmn|1dmn]], [[1dmq|1dmq]], [[1e3r|1e3r]], [[1e3v|1e3v]], [[1e97|1e97]], [[1ea2|1ea2]], [[1gs3|1gs3]], [[1k41|1k41]], [[1ogx|1ogx]], [[1oh0|1oh0]], [[1oho|1oho]], [[1opy|1opy]], [[1vzz|1vzz]], [[1w00|1w00]], [[1w01|1w01]], [[1w02|1w02]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Steroid_Delta-isomerase Steroid Delta-isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.3.1 5.3.3.1] </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=1w6y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w6y OCA], [http://pdbe.org/1w6y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1w6y RCSB], [http://www.ebi.ac.uk/pdbsum/1w6y PDBsum]</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=1w6y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w6y OCA], [http://pdbe.org/1w6y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1w6y RCSB], [http://www.ebi.ac.uk/pdbsum/1w6y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1w6y ProSAT]</span></td></tr>
 </table>
 == Evolutionary Conservation ==
@@ Line 12: / Line 13: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/w6/1w6y_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/w6/1w6y_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

1w6y

From Proteopedia

Revision as of 07:09, 4 April 2018

crystal structure of a mutant W92A in ketosteroid isomerase (KSI) from Pseudomonas putida biotype B

Structural highlights

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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