5WV3
Crystal structure of bovine lactoperoxidase with a partial Glu258-heme linkage at 2.07 A resolution.
Replaces: 5K1ESummary for 5WV3
| Entry DOI | 10.2210/pdb5wv3/pdb |
| Descriptor | Lactoperoxidase, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, CALCIUM ION, ... (10 entities in total) |
| Functional Keywords | oxidoreductase |
| Biological source | Bos taurus (Bovine) |
| Total number of polymer chains | 1 |
| Total formula weight | 71019.96 |
| Authors | Singh, P.K.,Sirohi, H.V.,Kaur, P.,Sharma, S.,Singh, T.P. (deposition date: 2016-12-21, release date: 2017-02-15, Last modification date: 2023-11-22) |
| Primary citation | Singh, P.K.,Iqbal, N.,Sirohi, H.V.,Bairagya, H.R.,Kaur, P.,Sharma, S.,Singh, T.P. Structural basis of activation of mammalian heme peroxidases Prog. Biophys. Mol. Biol., 133:49-55, 2018 Cited by PubMed Abstract: The mammalian heme peroxidases including lactoperoxidase (LPO), myeloperoxidase (MPO), eosinophil peroxidase (EPO) and thyroid peroxidase (TPO) contain a covalently linked heme moiety. Initially, it was believed that the heme group was fully cross-linked to protein molecule through at least two ester linkages involving conserved glutamate and aspartate residues with 1-methyl and 5-methyl groups of pyrrole rings A and C respectively. In MPO, an additional sulfonium ion linkage was present between 2-vinyl group of pyrrole ring A of the heme moiety and a methionine residue of the protein. These linkages were formed through a self processing mechanism. Subsequently, biochemical studies indicated that the heme moiety was partially attached to protein. The recent structural studies have shown that the covalent linkage involving glutamate and 1-methyl group of pyrrole ring of heme moiety was partially formed. When glutamate is not covalently linked to heme moiety, its side chain occupies a position in the substrate binding site on the distal heme side and blocks the substrate binding site leading to inactivation. However, an exposure to HO converts it to a fully covalently linked state with heme. Thus in mammalian heme peroxidases, the Glu-heme linkage is essential for catalytic action. PubMed: 29174286DOI: 10.1016/j.pbiomolbio.2017.11.003 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.07 Å) |
Structure validation
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