5hv4

Crystal Structure of a Prolyl 4-Hydroxylase Complexed with Alpha-ketoglutarate from the Pathogenic Bacterium Bacillus anthracis in C2221Crystal Structure of a Prolyl 4-Hydroxylase Complexed with Alpha-ketoglutarate from the Pathogenic Bacterium Bacillus anthracis in C2221

Structural highlights 5hv4 is a 1 chain structure with sequence from "bacillus_cereus_var._anthracis"_(cohn_1872)_smith_et_al._1946 "bacillus cereus var. anthracis" (cohn 1872) smith et al. 1946. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: , , Related: 5hv0 Gene: GBAA_4459, AB163_21210, AB164_16730, AB165_11640, AB166_03610, AB167_21505, AB168_05660, AB169_05325, AB170_09560, AB171_10145, AB893_21665, ADK17_22720, ADK18_21540, ADT20_05380, ADT21_14515, BF27_3254 ("Bacillus cereus var. anthracis" (Cohn 1872) Smith et al. 1946) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed The prolyl 4-hydroxylases (P4Hs) are mononuclear nonheme iron enzymes that catalyze the formation of 4R-hydroxyproline from many different substrates, with various biological implications. P4H is a key player in collagen accumulation, which has implications in fibrotic disorders. The stabilization of collagen triple-helical structure via prolyl hydroxylation is the rate-limiting step in collagen biosynthesis, and therefore P4H has been extensively investigated as a potential therapeutic target of fibrotic disease. Understanding how these enzymes recognize cofactors and substrates is important and will aid in the future design of inhibitors of P4H. In this article, X-ray crystal structures of a metallocofactor- and alpha-ketoglutarate (alphaKG)-bound form of P4H from Bacillus anthracis (BaP4H) are reported. Structures of BaP4H were solved at 1.63 and 2.35 A resolution and contained a cadmium ion and alphaKG bound in the active site. The alphaKG-Cd-BaP4H ternary complex reveals conformational changes of conserved residues upon the binding of metal ion and alphaKG, resulting in a closed active-site configuration required for dioxygen, substrate binding and catalysis. Structural analysis of cofactor binding for a prolyl 4-hydroxylase from the pathogenic bacterium Bacillus anthracis.,Schnicker NJ, Dey M Acta Crystallogr D Struct Biol. 2016 May 1;72(Pt 5):675-81. doi:, 10.1107/S2059798316004198. Epub 2016 Apr 26. PMID:27139630 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 5hv4, resolution 2.35Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image