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5kp4

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<StructureSection load='5kp4' size='340' side='right'caption='[[5kp4]], [[Resolution|resolution]] 1.71&Aring;' scene=''>
<StructureSection load='5kp4' size='340' side='right'caption='[[5kp4]], [[Resolution|resolution]] 1.71&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5kp4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_fluorescens_putidus"_flugge_1886 "bacillus fluorescens putidus" flugge 1886]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KP4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KP4 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5kp4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KP4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KP4 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=6VW:(8~{R},9~{S},10~{R},13~{S},14~{S},17~{S})-13-METHYL-17-OXIDANYL-2,6,7,8,9,10,11,12,14,15,16,17-DODECAHYDRO-1~{H}-CYCLOPENTA[A]PHENANTHREN-3-ONE'>6VW</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.706&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5d81|5d81]], [[5kp1|5kp1]], [[5kp3|5kp3]], [[5d82|5d82]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6VW:(8~{R},9~{S},10~{R},13~{S},14~{S},17~{S})-13-METHYL-17-OXIDANYL-2,6,7,8,9,10,11,12,14,15,16,17-DODECAHYDRO-1~{H}-CYCLOPENTA[A]PHENANTHREN-3-ONE'>6VW</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ksi ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=303 "Bacillus fluorescens putidus" Flugge 1886])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5kp4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kp4 OCA], [https://pdbe.org/5kp4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5kp4 RCSB], [https://www.ebi.ac.uk/pdbsum/5kp4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5kp4 ProSAT]</span></td></tr>
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<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>
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<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=5kp4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kp4 OCA], [http://pdbe.org/5kp4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kp4 RCSB], [http://www.ebi.ac.uk/pdbsum/5kp4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kp4 ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/SDIS_PSEPU SDIS_PSEPU]
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The vibrational Stark effect (VSE) has been used to measure the electric field in the active site of ketosteroid isomerase (KSI). These measured fields correlate with DeltaG in a series of conventional mutants, yielding an estimate for the electrostatic contribution to catalysis (Fried et al. Science 2014, 346, 1510-1513). In this work we test this result with much more conservative variants in which individual Tyr residues in the active site are replaced by 3-chlorotyrosine via amber suppression. The electric fields sensed at the position of the carbonyl bond involved in charge displacement during catalysis were characterized using the VSE, where the field sensitivity has been calibrated by vibrational Stark spectroscopy, solvatochromism, and MD simulations. A linear relationship is observed between the electric field and DeltaG that interpolates between wild-type and more drastic conventional mutations, reinforcing the evaluation of the electrostatic contribution to catalysis in KSI. A simplified model and calculation are developed to estimate changes in the electric field accompanying changes in the extended hydrogen-bond network in the active site. The results are consistent with a model in which the O-H group of a key active site tyrosine functions by imposing a static electrostatic potential onto the carbonyl bond. The model suggests that the contribution to catalysis from the active site hydrogen bonds is of similar weight to the distal interactions from the rest of the protein. A similar linear correlation was also observed between the proton affinity of KSI's active site and the catalytic rate, suggesting a direct connection between the strength of the H-bond and the electric field it exerts.
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A Critical Test of the Electrostatic Contribution to Catalysis with Noncanonical Amino Acids in Ketosteroid Isomerase.,Wu Y, Boxer SG J Am Chem Soc. 2016 Sep 1. PMID:27545569<ref>PMID:27545569</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5kp4" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Ketosteroid Isomerase|Ketosteroid Isomerase]]
*[[Ketosteroid Isomerase|Ketosteroid Isomerase]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bacillus fluorescens putidus flugge 1886]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Steroid Delta-isomerase]]
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[[Category: Pseudomonas putida]]
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[[Category: Boxer, S G]]
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[[Category: Boxer SG]]
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[[Category: Wu, Y]]
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[[Category: Wu Y]]
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[[Category: Isomerase]]
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Current revision

Crystal Structure of Ketosteroid Isomerase from Pseudomonas putida (pKSI) bound to 19-nortestosterone

PDB ID 5kp4

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