4pnx

Crystal structure of the complex of lactoperoxidase with bromo methane at 2.41 angstrom resolution

spinqualitylabelsall models 4pnx, resolution 2.41Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4pnx is a 1 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BMM, CA, HEM, IOD, NAG, SEP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PERL_BOVIN LPO is an antimicrobial agent. It is thought to help protect the udder from infection and promote growth in newborn calves. Publication Abstract from PubMed Lactoperoxidase (LPO) is a member of mammalian heme peroxidase superfamily whose other members are myeloperoxidase (MPO), eosinophil peroxidase (EPO) and thyroid peroxidase (TPO). In these enzymes, the heme moiety is linked to protein through two or three covalent bonds. In the mature LPO, the heme moiety is linked to protein through two ester bonds with highly conserved glutamate and aspartate residues. The previously reported structures of LPO have confirmed the formation of two covalent linkages involving Glu258 and Asp108 with 1-methyl and 5-methyl groups of pyrrole rings A and C respectively. We report here a new form of structure of LPO where the covalent bond between Glu258 and 1-methyl group of pyrrole ring A is present only in a fraction of protein molecules. In this case, the side chain of Glu258 occupies two distinct positions, each of which has a 0.5 occupancy. In one position, it forms a normal ester covalent linkage while in the second position, the side chain of Glu258 is located in the middle of the substrate binding site on the distal heme side. In this position, the atom of the side chain of Glu258 forms several contacts with atoms of other residues and heme moiety. Out of the two observed positions of the side chain of Glu258, the former contributes to the stabilization of heme position and improved catalytic action of LPO while the latter is responsible for the reduced stability of the heme position as well as it blocks the substrate binding site. Structure of bovine lactoperoxidase with a partially linked heme moiety at 1.98A resolution.,Singh PK, Sirohi HV, Iqbal N, Tiwari P, Kaur P, Sharma S, Singh TP Biochim Biophys Acta. 2016 Dec 13;1865(3):329-335. doi:, 10.1016/j.bbapap.2016.12.006. PMID:27986533 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Lactoperoxidase

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