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| | == Structural highlights == | | == Structural highlights == |
| | <table><tr><td colspan='2'>[[2r5l]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Capra_hircus Capra hircus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2R5L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2R5L FirstGlance]. <br> | | <table><tr><td colspan='2'>[[2r5l]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Capra_hircus Capra hircus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2R5L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2R5L FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2pt3|2pt3]], [[2pum|2pum]]</div></td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Peroxidase Peroxidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.7 1.11.1.7] </span></td></tr>
| + | |
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2r5l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r5l OCA], [https://pdbe.org/2r5l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2r5l RCSB], [https://www.ebi.ac.uk/pdbsum/2r5l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2r5l ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2r5l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r5l OCA], [https://pdbe.org/2r5l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2r5l RCSB], [https://www.ebi.ac.uk/pdbsum/2r5l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2r5l ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/PERL_CAPHI PERL_CAPHI] Antimicrobial agent which utilizes hydrogen peroxide and thiocyanate (SCN) to generate the antimicrobial substance hypothiocyanous acid (HOSCN) (PubMed:10894086). May protect the udder from infection and promote growth in newborns. Inhibits growth of several fungi including A.niger, Trichoderma species, C.cassicola, P.meadii and C.salmonicolor (PubMed:10894086). Does not have anti-fungal activity towards C.albicans and Pythium species (PubMed:10894086). Inhibits growth of several Gram-positive bacteria including some Staphylococcus species and Gram-negative bacteria including E.coli, P.aeruginosa and some Salmonella species (PubMed:10894086).<ref>PMID:10894086</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | [[Category: Capra hircus]] | | [[Category: Capra hircus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Peroxidase]]
| + | [[Category: Kaur P]] |
| - | [[Category: Kaur, P]] | + | [[Category: Sharma S]] |
| - | [[Category: Sharma, S]] | + | [[Category: Singh AK]] |
| - | [[Category: Singh, A K]] | + | [[Category: Singh N]] |
| - | [[Category: Singh, N]] | + | [[Category: Singh TP]] |
| - | [[Category: Singh, T P]] | + | [[Category: Srinivasan A]] |
| - | [[Category: Srinivasan, A]] | + | |
| - | [[Category: Anion]]
| + | |
| - | [[Category: Heme]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
2r5l is a 1 chain structure with sequence from Capra hircus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 2.4Å |
| Ligands: | , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
PERL_CAPHI Antimicrobial agent which utilizes hydrogen peroxide and thiocyanate (SCN) to generate the antimicrobial substance hypothiocyanous acid (HOSCN) (PubMed:10894086). May protect the udder from infection and promote growth in newborns. Inhibits growth of several fungi including A.niger, Trichoderma species, C.cassicola, P.meadii and C.salmonicolor (PubMed:10894086). Does not have anti-fungal activity towards C.albicans and Pythium species (PubMed:10894086). Inhibits growth of several Gram-positive bacteria including some Staphylococcus species and Gram-negative bacteria including E.coli, P.aeruginosa and some Salmonella species (PubMed:10894086).[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Lactoperoxidase (LPO) is a member of the mammalian peroxidase superfamily. It catalyzes the oxidation of thiocyanate and halides. Freshly isolated and purified samples of caprine LPO were saturated with ammonium iodide and crystallized using 20% polyethylene glycol 3350 in a hanging drop vapor diffusion setup. The structure has been determined using X-ray crystallographic method and refined to R(cryst) and R(free) factors of 0.196 and 0.203, respectively. The structure determination revealed an unexpected phosphorylation of Ser198 in LPO, which is also confirmed by anti-phosphoserine antibody binding studies. The structure is also notable for observing densities for glycan chains at all the four potential glycosylation sites. Caprine LPO consists of a single polypeptide chain of 595 amino acid residues and folds into an oval-shaped structure. The structure contains 20 well-defined alpha-helices of varying lengths including a helix, H(2a), unique to LPO, and two short antiparallel beta-strands. The structure confirms that the heme group is covalently linked to the protein through two ester linkages involving carboxylic groups of Glu258 and Asp108 and modified methyl groups of pyrrole rings A and C, respectively. The heme moiety is slightly distorted from planarity, but pyrrole ring B is distorted considerably. However, an iron atom is displaced only by 0.1 A from the plane of the heme group toward the proximal site. The substrate diffusing channel in LPO is cylindrical in shape with a diameter of approximately 6 A. Two histidine residues and six buried water molecules are connected through a hydrogen-bonded chain from the distal heme cavity to the surface of protein molecule and seemingly form the basis of proton relay for catalytic action. Ten iodide ions have been observed in the structure. Out of these, only one iodide ion is located in the distal heme cavity and is hydrogen bonded to the water molecule W1. W1 is also hydrogen bonded to the heme iron as well as to distal His109. The structure contains a calcium ion that is coordinated to seven oxygen atoms and forms a typical pentagonal bipyramidal coordination geometry.
Crystal structure of lactoperoxidase at 2.4 A resolution.,Singh AK, Singh N, Sharma S, Singh SB, Kaur P, Bhushan A, Srinivasan A, Singh TP J Mol Biol. 2008 Feb 29;376(4):1060-75. Epub 2007 Dec 14. PMID:18191143[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Benoy MJ, Essy AK, Sreekumar B, Haridas M. Thiocyanate mediated antifungal and antibacterial property of goat milk lactoperoxidase. Life Sci. 2000;66(25):2433-9. doi: 10.1016/s0024-3205(00)80003-x. PMID:10894086 doi:http://dx.doi.org/10.1016/s0024-3205(00)80003-x
- ↑ Singh AK, Singh N, Sharma S, Singh SB, Kaur P, Bhushan A, Srinivasan A, Singh TP. Crystal structure of lactoperoxidase at 2.4 A resolution. J Mol Biol. 2008 Feb 29;376(4):1060-75. Epub 2007 Dec 14. PMID:18191143 doi:10.1016/j.jmb.2007.12.012
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