3v6q: Difference between revisions
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The | ==Crystal structure of the complex of bovine lactoperoxidase with Carbon monoxide at 2.0 A resolution== | ||
<StructureSection load='3v6q' size='340' side='right'caption='[[3v6q]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3v6q]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3V6Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3V6Q FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SCN:THIOCYANATE+ION'>SCN</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></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=3v6q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v6q OCA], [https://pdbe.org/3v6q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3v6q RCSB], [https://www.ebi.ac.uk/pdbsum/3v6q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3v6q ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/PERL_BOVIN PERL_BOVIN] LPO is an antimicrobial agent. It is thought to help protect the udder from infection and promote growth in newborn calves. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Lactoperoxidase (LPO) is a hemeprotein catalyzing the oxidation of thiocyanate and I(-) into antimicrobials and small aromatic organics after being itself oxidized by H(2)O(2). LPO is excreted by the lungs, mammary glands, found in saliva and tears and protects mammals against bacterial, fungal and viral invasion. The Fe(II) form binds CO which inactivates LPO like many other hemeproteins. We present the 3-dimensional structure of CO-LPO at 2.0A resolution and infrared (IR) spectra of the iron-bound CO stretch from pH 3 to 8.8 at 1 cm(-1) resolution. The observed Fe-C-O bond angle of 132 degrees is more acute than the electronically related Fe(III), CN-LPO with a Fe-C-N angle of 161 degrees . The orientations of the two ligands are different with the oxygen of CO pointing towards the imidazole of distal His109 while the nitrogen of CN points away, the Fe(II) moves towards His109 while the Fe(III) moves away; both movements are consistent with a hydrogen bond between the distal His109 and CO, but not to the nitrogen of CN-LPO. The IR spectra of CO-LPO exhibit two major CO absorbances with pH dependent relative intensities. Both crystallographic and IR data suggest proton donation to the CO oxygen by His109 with a pK approximately 4; close to the pH of greatest enzyme turnover. The IR absorbance maxima are consistent with a first order correlation between frequency and Fe(III)/Fe(II) reduction potential at pH 7; both band widths at half-height correlate with electron density donation from Fe(II) to CO as gauged by the reduction potential. | |||
Bovine carbonyl lactoperoxidase structure at 2.0A resolution and infrared spectra as a function of pH.,Singh AK, Smith ML, Yamini S, Ohlsson PI, Sinha M, Kaur P, Sharma S, Paul JA, Singh TP, Paul KG Protein J. 2012 Oct;31(7):598-608. doi: 10.1007/s10930-012-9436-3. PMID:22886082<ref>PMID:22886082</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3v6q" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Lactoperoxidase|Lactoperoxidase]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bos taurus]] | |||
[[Category: Large Structures]] | |||
[[Category: Kaur P]] | |||
[[Category: Pandey N]] | |||
[[Category: Sharma S]] | |||
[[Category: Singh AK]] | |||
[[Category: Singh TP]] | |||
[[Category: Sinha M]] | |||
[[Category: Yamini S]] | |||
Latest revision as of 09:15, 17 October 2024
Crystal structure of the complex of bovine lactoperoxidase with Carbon monoxide at 2.0 A resolutionCrystal structure of the complex of bovine lactoperoxidase with Carbon monoxide at 2.0 A resolution
Structural highlights
FunctionPERL_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 PubMedLactoperoxidase (LPO) is a hemeprotein catalyzing the oxidation of thiocyanate and I(-) into antimicrobials and small aromatic organics after being itself oxidized by H(2)O(2). LPO is excreted by the lungs, mammary glands, found in saliva and tears and protects mammals against bacterial, fungal and viral invasion. The Fe(II) form binds CO which inactivates LPO like many other hemeproteins. We present the 3-dimensional structure of CO-LPO at 2.0A resolution and infrared (IR) spectra of the iron-bound CO stretch from pH 3 to 8.8 at 1 cm(-1) resolution. The observed Fe-C-O bond angle of 132 degrees is more acute than the electronically related Fe(III), CN-LPO with a Fe-C-N angle of 161 degrees . The orientations of the two ligands are different with the oxygen of CO pointing towards the imidazole of distal His109 while the nitrogen of CN points away, the Fe(II) moves towards His109 while the Fe(III) moves away; both movements are consistent with a hydrogen bond between the distal His109 and CO, but not to the nitrogen of CN-LPO. The IR spectra of CO-LPO exhibit two major CO absorbances with pH dependent relative intensities. Both crystallographic and IR data suggest proton donation to the CO oxygen by His109 with a pK approximately 4; close to the pH of greatest enzyme turnover. The IR absorbance maxima are consistent with a first order correlation between frequency and Fe(III)/Fe(II) reduction potential at pH 7; both band widths at half-height correlate with electron density donation from Fe(II) to CO as gauged by the reduction potential. Bovine carbonyl lactoperoxidase structure at 2.0A resolution and infrared spectra as a function of pH.,Singh AK, Smith ML, Yamini S, Ohlsson PI, Sinha M, Kaur P, Sharma S, Paul JA, Singh TP, Paul KG Protein J. 2012 Oct;31(7):598-608. doi: 10.1007/s10930-012-9436-3. PMID:22886082[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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