3fjn

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{{Seed}}
 
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[[Image:3fjn.png|left|200px]]
 
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==The crystal structure of 17-alpha hydroxysteroid dehydrogenase Y224D mutant.==
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The line below this paragraph, containing "STRUCTURE_3fjn", creates the "Structure Box" on the page.
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<StructureSection load='3fjn' size='340' side='right'caption='[[3fjn]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3fjn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FJN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FJN FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2.3&#8491;</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=ACT:ACETATE+ION'>ACT</scene></td></tr>
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{{STRUCTURE_3fjn| PDB=3fjn | SCENE= }}
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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=3fjn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fjn OCA], [https://pdbe.org/3fjn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fjn RCSB], [https://www.ebi.ac.uk/pdbsum/3fjn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fjn ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/AK1CL_MOUSE AK1CL_MOUSE] NADP-dependent 17-alpha-hydroxysteroid dehydrogenase that converts 5-alpha-androstane-3,17-dione into androsterone. Has lower 3-alpha-hydroxysteroid dehydrogenase activity. Has broad substrate specificity and acts on various 17-alpha-hydroxysteroids, 17-ketosteroids, 3-alpha hydroxysteroids and 3-ketosteroids. Reduction of keto groups is strictly stereoselective. Reduction of 17-ketosteroids yields only 17-alpha-hydroxysteroids. Likewise, reduction of 3-ketosteroids yields only 3-alpha-hydroxysteroids.<ref>PMID:15577209</ref> <ref>PMID:16018803</ref> <ref>PMID:17034817</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fj/3fjn_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=3fjn ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Mouse 3(17)alpha-hydroxysteroid dehydrogenase (AKR1C21) is the only aldo-keto reductase that catalyzes the stereospecific reduction of 3- and 17-ketosteroids to the corresponding 3(17)alpha-hydroxysteroids. The Y224D mutation of AKR1C21 reduced the K(m) value for NADP(H) by up to 80-fold and completely reversed the 17alpha stereospecificity of the enzyme. The crystal structure of the Y224D mutant at 2.3 A resolution revealed that the mutation resulted in a change in the conformation of the flexible loop B, including the V-shaped groove, which is a unique feature of the active-site architecture of wild-type AKR1C21 and is formed by the side chains of Tyr224 and Trp227. Furthermore, mutations (Y224F and Q222N) of residues involved in forming the safety belt for binding of the coenzyme showed similar alterations in kinetic constants for 3alpha-hydroxy/3-ketosteroids and 17-hydroxy/ketosteroids compared with the wild type.
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===The crystal structure of 17-alpha hydroxysteroid dehydrogenase Y224D mutant.===
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Studies on a Tyr residue critical for the binding of coenzyme and substrate in mouse 3(17)alpha-hydroxysteroid dehydrogenase (AKR1C21): structure of the Y224D mutant enzyme.,Dhagat U, Endo S, Mamiya H, Hara A, El-Kabbani O Acta Crystallogr D Biol Crystallogr. 2010 Feb;66(Pt 2):198-204. Epub 2010, Jan 22. PMID:20124700<ref>PMID:20124700</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 3fjn" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_20124700}}, adds the Publication Abstract to the page
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*[[Hydroxysteroid dehydrogenase 3D structures|Hydroxysteroid dehydrogenase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 20124700 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_20124700}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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3FJN is a 2 chains structure with sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FJN OCA].
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==Reference==
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<ref group="xtra">PMID:20124700</ref><references group="xtra"/>
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Dhagat, U.]]
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[[Category: Dhagat U]]
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[[Category: El-Kabbani, O.]]
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[[Category: El-Kabbani O]]
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[[Category: 17-alpha-hydroxysteroid dehydrogenase]]
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[[Category: Aldo-keto reductase]]
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[[Category: Cytoplasm]]
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[[Category: Lipid metabolism]]
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[[Category: Nadp]]
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[[Category: Oxidoreductase]]
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[[Category: Phosphoprotein]]
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[[Category: Steroid metabolism]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 17 09:49:47 2010''
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Current revision

The crystal structure of 17-alpha hydroxysteroid dehydrogenase Y224D mutant.

PDB ID 3fjn

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