7de5

Crystal structure of yak lactoperoxidase at 1.55 A resolution.Crystal structure of yak lactoperoxidase at 1.55 A resolution.

Structural highlights 7de5 is a 1 chain structure with sequence from Bos grunniens. This structure supersedes the now removed PDB entries 7ch2, 7byz and 6l2v. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.55Å Ligands: , , , , , , , Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function L8ICE9_9CETA Publication Abstract from PubMed Lactoperoxidase (LPO) is a heme containing oxido-reductase enzyme. It is secreted from mammary, salivary, lachrymal and mucosal glands. It catalyses the conversion of thiocyanate into hypothiocyanate and halides into hypohalides. LPO belongs to the superfamily of mammalian heme peroxidases which also includes myeloperoxidase (MPO), eosinophil peroxidase (EPO) and thyroid peroxidase (TPO). The heme prosthetic group is covalently linked in LPO through two ester bonds involving conserved residues Glu258 and Asp108. It was isolated from colostrum of yak (Bos grunniens), purified to homogeneity and crystallized using ammonium iodide as a precipitating agent. The crystals belonged to monoclinic space group P2(1) with cell dimensions of a = 53.91 A, b = 78.98 A, c = 67.82 A and beta = 92.96 degrees . The structure was determined at 1.55 A resolution. This is the first structure of LPO from yak. Also, this is the highest resolution structure of LPO determined so far from any source. The structure determination revealed that three segments (Ser1-Cys15), (Thr117-Asn138) and (Cys167-Leu175) were disordered and formed one surface of LPO structure. In the substrate binding site, the iodide ions were observed in three subsites which are formed by (1) heme moiety and residues, Gln105, Asp108, His109, Phe113, Arg255, Glu258, Phe380 and Phe381, (2) residues, Asn230, Lys232, Pro236, Cys248, Phe254, Phe381 and Pro424 and (3) residues, Ser198, Leu199 and Arg202. The structure determination also revealed that the side chain of Phe254 was disordered. It was observed to adopt two conformations in the structures of LPO. Structure of Yak Lactoperoxidase at 1.55 A Resolution.,Viswanathan V, Rani C, Ahmad N, Singh PK, Sharma P, Kaur P, Sharma S, Singh TP Protein J. 2021 Feb;40(1):8-18. doi: 10.1007/s10930-020-09957-2. Epub 2021 Jan 3. PMID:33389415 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Lactoperoxidase

spinqualitylabelsall models 7de5, resolution 1.55Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image