6qck - Revision history

OCA at 11:57, 24 January 2024

2024-01-24T11:57:51Z

←Older revision		Revision as of 11:57, 24 January 2024
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	<StructureSection load='6qck' size='340' side='right'caption='[[6qck]], [[Resolution\|resolution]] 1.68Å' scene=''>		<StructureSection load='6qck' size='340' side='right'caption='[[6qck]], [[Resolution\|resolution]] 1.68Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6qck]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QCK OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=6QCK FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6qck]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QCK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6QCK FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=HWK:2-[2-(1,3-benzodioxol-2-yl)ethyl]benzoic+acid'>HWK</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></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]] 1.68Å</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=6qck FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qck OCA], [~~http~~://pdbe.org/6qck PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6qck RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6qck PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6qck ProSAT]</span></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=HWK:2-[2-(1,3-benzodioxol-2-yl)ethyl]benzoic+acid'>HWK</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></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=6qck FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qck OCA], [https://pdbe.org/6qck PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6qck RCSB], [https://www.ebi.ac.uk/pdbsum/6qck PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6qck ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/DHB14_HUMAN DHB14_HUMAN]] Has NAD-dependent 17-beta-hydroxysteroid dehydrogenase activity. Converts oestradiol to oestrone. The physiological substrate is not known. Acts on oestradiol and 5-androstene-3-beta,17-beta-diol (in vitro).<ref>PMID:17067289</ref>	+	[https://www.uniprot.org/uniprot/DHB14_HUMAN DHB14_HUMAN] Has NAD-dependent 17-beta-hydroxysteroid dehydrogenase activity. Converts oestradiol to oestrone. The physiological substrate is not known. Acts on oestradiol and 5-androstene-3-beta,17-beta-diol (in vitro).<ref>PMID:17067289</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	17beta-Hydroxysteroid dehydrogenase type 14 (17beta-HSD14) catalyzes the conversion of highly active estrogens and androgens into their less active oxidized forms in presence of NAD(+) as cofactor. The crystal structure of 17beta-HSD14 has been determined, however, the role of individual amino acids likely involved in the enzymatic function remains poorly understood. Objective of this study was to further characterize the enzyme by site-directed mutagenesis considering five amino acids next to the catalytic center. The tools used for the characterization of the enzyme variants are X-ray crystallography and enzyme kinetics. Lys158 was confirmed to belong to the catalytic triad. Tyr253', located on the C-terminal loop of the adjacent monomer, enters into the active site of the neighboring monomer and interacts with the catalytic Tyr154. Therefore, Tyr253' helps to tie the two monomers together. Cys255, located at the interface between both monomers, can form a disulfide bridge with the Cys255' from the adjacent monomer. In contrast to the contact provided by Tyr253, the latter interaction is not crucial for dimer formation. His93 and Gln148 are located at the rim of the substrate binding pocket. His93 does not interact directly with the ligand in the active site. However, it influences the turnover of the enzyme. The Gln148 restricts in size the access tunnel of the substrate to the binding pocket.
		+
		+	Mutational and structural studies uncover crucial amino acids determining activity and stability of 17beta-HSD14.,Badran MJ, Bertoletti N, Keils A, Heine A, Klebe G, Marchais-Oberwinkler S J Steroid Biochem Mol Biol. 2019 May;189:135-144. doi:, 10.1016/j.jsbmb.2019.02.009. Epub 2019 Mar 2. PMID:30836176<ref>PMID:30836176</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 6qck" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Hydroxysteroid dehydrogenase 3D structures\|Hydroxysteroid dehydrogenase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Bertoletti, N]]	+	[[Category: Bertoletti N]]
-	[[Category: Heine, A]]	+	[[Category: Heine A]]
-	[[Category: Klebe, G]]	+	[[Category: Klebe G]]
-	[[Category: Marchais-Oberwinkler, S]]	+	[[Category: Marchais-Oberwinkler S]]
-	~~[[Category: 17b-hsd14]]~~	+
-	~~[[Category: Fragment]]~~	+
-	~~[[Category: Oxidoreductase]]~~	+
-	~~[[Category: Soaking~~]]	+

OCA at 15:35, 29 January 2020

2020-01-29T15:35:05Z

←Older revision		Revision as of 15:35, 29 January 2020
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-	'''Unreleased structure'''

-	~~The entry~~ 6qck ~~is ON HOLD~~	+	==17beta-hydroxysteroid dehydrogenase 14 variant T205 in complex with FB262==
-		+	<StructureSection load='6qck' size='340' side='right'caption='[[6qck]], [[Resolution\|resolution]] 1.68Å' scene=''>
-	~~Authors~~: ~~Bertoletti, N~~., ~~Marchais~~-~~Oberwinkler~~, S., ~~Heine~~, A., ~~Klebe~~, G.	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[6qck]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QCK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6QCK FirstGlance]. <br>
-	~~Description~~: ~~17beta~~-hydroxysteroid dehydrogenase ~~14 variant T205~~ in ~~complex with FB262~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=HWK:2-[2-(1,3-benzodioxol-2-yl)ethyl]benzoic+acid'>HWK</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr>
-	[[Category: ~~Unreleased~~ Structures]]	+	<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=6qck FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qck OCA], [http://pdbe.org/6qck PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6qck RCSB], [http://www.ebi.ac.uk/pdbsum/6qck PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6qck ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/DHB14_HUMAN DHB14_HUMAN]] Has NAD-dependent 17-beta-hydroxysteroid dehydrogenase activity. Converts oestradiol to oestrone. The physiological substrate is not known. Acts on oestradiol and 5-androstene-3-beta,17-beta-diol (in vitro).<ref>PMID:17067289</ref>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Bertoletti, N]]
	[[Category: Heine, A]]		[[Category: Heine, A]]
-	[[Category: ~~Bertoletti~~, N]]	+	[[Category: Klebe, G]]
	[[Category: Marchais-Oberwinkler, S]]		[[Category: Marchais-Oberwinkler, S]]
-	[[Category: ~~Klebe, G~~]]	+	[[Category: 17b-hsd14]]
		+	[[Category: Fragment]]
		+	[[Category: Oxidoreductase]]
		+	[[Category: Soaking]]

OCA: Protected "6qck" [edit=sysop:move=sysop]

2019-01-09T05:09:04Z

Protected "6qck" [edit=sysop:move=sysop]

←Older revision

Revision as of 05:09, 9 January 2019

OCA: New page: '''Unreleased structure''' The entry 6qck is ON HOLD Authors: Bertoletti, N., Marchais-Oberwinkler, S., Heine, A., Klebe, G. Description: 17beta-hydroxysteroid dehydrogenase 14 variant...

2019-01-09T05:09:02Z

New page: '''Unreleased structure''' The entry 6qck is ON HOLD Authors: Bertoletti, N., Marchais-Oberwinkler, S., Heine, A., Klebe, G. Description: 17beta-hydroxysteroid dehydrogenase 14 variant...

New page

'''Unreleased structure'''

The entry 6qck is ON HOLD

Authors: Bertoletti, N., Marchais-Oberwinkler, S., Heine, A., Klebe, G.

Description: 17beta-hydroxysteroid dehydrogenase 14 variant T205 in complex with FB262
[[Category: Unreleased Structures]]
[[Category: Heine, A]]
[[Category: Bertoletti, N]]
[[Category: Marchais-Oberwinkler, S]]
[[Category: Klebe, G]]