5fyd | pdb_00005fyd

Structural and biochemical insights into 7beta-hydroxysteroid dehydrogenase stereoselectivity

spinqualitylabelsall models 5fyd, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5fyd is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GOL Activity: 7-beta-hydroxysteroid dehydrogenase (NADP(+)), with EC number 1.1.1.201 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Publication Abstract from PubMed Hydroxysteroid dehydrogenases are of great interest as biocatalysts for transformations involving steroid substrates. They feature a high degree of stereo- and regio-selectivity, acting on a defined atom with a specific configuration of the steroid nucleus. The crystal structure of 7beta-hydroxysteroid dehydrogenase from Collinsella aerofaciens reveals a loop gating active-site accessibility, the bases of the specificity for NADP+ , and the general architecture of the steroid binding site. Comparison with 7alpha-hydroxysteroid dehydrogenase provides a rationale for the opposite stereoselectivity. The presence of a C-terminal extension reshapes the substrate site of the beta-selective enzyme, possibly leading to an inverted orientation of the bound substrate. This article is protected by copyright. All rights reserved. Structural and biochemical insights into 7beta-hydroxysteroid dehydrogenase stereoselectivity.,Savino S, Ferrandi EE, Forneris F, Rovida S, Riva S, Monti D, Mattevi A Proteins. 2016 Mar 23. doi: 10.1002/prot.25036. PMID:27006087 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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