Structural highlights
4qdf is a 2 chain structure with sequence from Rhodococcus rhodochrous. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Method: | X-ray diffraction, Resolution 2.43Å |
| Ligands: | , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
KSHA5_RHORH Probably involved in the degradation of cholesterol (PubMed:21642460). In vitro, catalyzes the introduction of a 9alpha-hydroxyl moiety into the ring B of 3-ketosteroid substrates such as 1,4-androstadiene-3,17-dione (ADD), 4-androstene-3,17-dione (AD), 4-androstene-17beta-ol-3-one (testosterone), 4-pregnene-3,20-dione (progesterone), 19-nor-4-androstene-3,17-dione, 1-(5alpha)-androstene-3,17-dione, 5alpha-androstane-3,17-dione, 5beta-androstane-3,17-dione, 5alpha-androstane-17beta-ol-3-one (stanolon), 11beta-hydrocortisone, 3-oxo-23,24-bisnorcholesta-4-en-22-oate (4-BNC), 23,24-bisnorcholesta-4-ene-22-oate, 3-oxo-23,24-bisnorcholesta-1,4-dien-22-oate (1,4-BNC) and 3-oxo-23,24-bisnorcholesta-1,4-dien-22-oyl-coenzyme A thioester (1,4-BNC-CoA) (PubMed:21642460, PubMed:25049233). KshA5 has the broadest substrate range without a clear substrate preference and is active with Delta-4, Delta-1,4, 5alpha-H and 5beta-H steroids, as well as with steroids having bulky aliphatic side chains and an isopropionyl side chain at C17.[1] [2]
References
- ↑ Petrusma M, Hessels G, Dijkhuizen L, van der Geize R. Multiplicity of 3-Ketosteroid-9α-Hydroxylase enzymes in Rhodococcus rhodochrous DSM43269 for specific degradation of different classes of steroids. J Bacteriol. 2011 Aug;193(15):3931-40. PMID:21642460 doi:10.1128/JB.00274-11
- ↑ Penfield JS, Worrall LJ, Strynadka NC, Eltis LD. Substrate specificities and conformational flexibility of 3-ketosteroid 9alpha-hydroxylases. J Biol Chem. 2014 Sep 12;289(37):25523-36. doi: 10.1074/jbc.M114.575886. Epub, 2014 Jul 21. PMID:25049233 doi:http://dx.doi.org/10.1074/jbc.M114.575886
