6ow4
From Proteopedia
(Difference between revisions)
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<StructureSection load='6ow4' size='340' side='right'caption='[[6ow4]], [[Resolution|resolution]] 1.99Å' scene=''> | <StructureSection load='6ow4' size='340' side='right'caption='[[6ow4]], [[Resolution|resolution]] 1.99Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6ow4]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OW4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6OW4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6ow4]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Bifidobacterium_adolescentis_l2-32 Bifidobacterium adolescentis l2-32]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OW4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6OW4 FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BIFADO_01909 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=411481 Bifidobacterium adolescentis L2-32])</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=6ow4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ow4 OCA], [http://pdbe.org/6ow4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ow4 RCSB], [http://www.ebi.ac.uk/pdbsum/6ow4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ow4 ProSAT]</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=6ow4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ow4 OCA], [http://pdbe.org/6ow4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ow4 RCSB], [http://www.ebi.ac.uk/pdbsum/6ow4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ow4 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Anaerobic bacteria inhabiting the human gastrointestinal tract have evolved various enzymes that modify host-derived steroids. The bacterial steroid-17,20-desmolase pathway cleaves the cortisol side-chain, forming pro-androgens predicted to impact host physiology. Bacterial 20beta-hydroxysteroid dehydrogenase (20beta-HSDH) regulates cortisol side-chain cleavage by reducing the C-20 carboxyl group on cortisol, yielding 20beta-dihydrocortisol. Recently, the gene encoding 20beta-HSDH in Butyricicoccus desmolans ATCC 43058 was reported, and a non-redundant protein search yielded a candidate 20beta-HSDH gene in Bifidobacterium adolescentis strain L2-32. B. adolescentis 20beta-HSDH could regulate cortisol side-chain cleavage by limiting pro-androgen formation in bacteria such as Clostridium scindens and 21-dehydroxylation by Eggerthella lenta Here, the putative B. adolescentis 20beta-HSDH was cloned, overexpressed and purified. 20beta-HSDH activity was confirmed through whole cell and pure enzymatic assays and it is specific for cortisol. Next, we solved the structures of recombinant 20beta-HSDH in both the apo and holo forms at 2.0-2.2A resolutions, revealing close overlap except for rearrangements near the active site. Interestingly, the structures contain a large, flexible N-terminal region which was investigated by gel filtration chromatography and CD spectroscopy. This extended N-terminus is important for protein stability because deletions of varying lengths caused structural changes and reduced enzymatic activity. A nonconserved extended N-terminus was also observed in several short-chain dehydro-genase/reductase family members. B. adolescentis strains capable of 20beta-HSDH activity could alter glucocorticoid metabolism in the gut and thereby serve as potential probiotics for the management of androgen-dependent diseases. | ||
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| + | Structural and biochemical characterization of 20beta-hydroxysteroid dehydrogenase from Bifidobacterium adolescentis strain L2-32.,Doden HL, Pollet RM, Mythen SM, Wawrzak Z, Devendran S, Cann I, Koropatkin NM, Ridlon JM J Biol Chem. 2019 Jun 17. pii: RA119.009390. doi: 10.1074/jbc.RA119.009390. PMID:31209107<ref>PMID:31209107</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6ow4" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Bifidobacterium adolescentis l2-32]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Koropatkin, N M]] | [[Category: Koropatkin, N M]] | ||
Revision as of 06:35, 10 July 2019
Structure of the NADH-bound form of 20beta-Hydroxysteroid Dehydrogenase from Bifidobacterium adolescentis strain L2-32
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