Journal:Acta Cryst D:S2059798322007082
From Proteopedia
(Difference between revisions)
| Line 4: | Line 4: | ||
<hr/> | <hr/> | ||
<b>Molecular Tour</b><br> | <b>Molecular Tour</b><br> | ||
| - | The human enzyme myeloperoxidase (MPO in short) is a heme-dependent peroxidase. The peroxidases are a large group of enzymes playing roles in various biological processes. MPO is found in mammalian neutrophils, which is a type of with blood cells, and there it catalyzes the oxidation of halide ions and thiocyanate in the presence of hydrogen peroxide. This results in strong oxidizing agents and they are helping to eliminate the bacteria or viruses which were taken up by phagocytosis. So, MPO is a key protein in the human immune defense system. | + | The human enzyme myeloperoxidase (MPO in short) is a heme-dependent peroxidase. The peroxidases are a large group of enzymes playing roles in various biological processes. MPO is found in mammalian neutrophils, which is a type of with blood cells, and there it catalyzes the oxidation of halide ions and thiocyanate in the presence of hydrogen peroxide. This results in strong oxidizing agents and they are helping to eliminate the bacteria or viruses which were taken up by phagocytosis. So, MPO is a key protein in the human immune defense system. <scene name='91/917471/Cv/12'>TextToBeDisplayed</scene> |
In order for MPO to function correctly, sugar molecules need to be present on its protein surface. This is called the glycosylation pattern. Until now, only a part of the glycosylation of MPO could be seen from the crystal structures deposited in the Protein Data Bank, holding the collection of available structures of biomolecules. Human MPO has five glycosylation sites, identified at positions Asn323, Asn355, Asn391, Asn483 and Asn729. We present here a structure in which the glycan structures on these five glycosylation sites could be identified. <scene name='91/917471/Cv/8'>The final model contains 8 polypeptide chains of mature MPO</scene> and 30 glycan chains on the Asn-binding sites. Each chain has a different colour. The 8 monomers forming <scene name='91/917471/Cv/7'>4 biological assemblies as homodimers AB, CD, EF and GH</scene> (each dimer has a different colour) in the crystal structure of human MPO, with their glycosylation structures as determined. <scene name='91/917471/Cv/10'>Monomers A, D, F and H have a bound paroxetine inhibitor</scene> (magenta), and each catalytic site carries an iron-containing <scene name='91/917471/Cv/11'>heme group</scene> (sea-green). We compare these with the glycans identified in proteomics studies and from eighteen human MPO structures available in the PDB. | In order for MPO to function correctly, sugar molecules need to be present on its protein surface. This is called the glycosylation pattern. Until now, only a part of the glycosylation of MPO could be seen from the crystal structures deposited in the Protein Data Bank, holding the collection of available structures of biomolecules. Human MPO has five glycosylation sites, identified at positions Asn323, Asn355, Asn391, Asn483 and Asn729. We present here a structure in which the glycan structures on these five glycosylation sites could be identified. <scene name='91/917471/Cv/8'>The final model contains 8 polypeptide chains of mature MPO</scene> and 30 glycan chains on the Asn-binding sites. Each chain has a different colour. The 8 monomers forming <scene name='91/917471/Cv/7'>4 biological assemblies as homodimers AB, CD, EF and GH</scene> (each dimer has a different colour) in the crystal structure of human MPO, with their glycosylation structures as determined. <scene name='91/917471/Cv/10'>Monomers A, D, F and H have a bound paroxetine inhibitor</scene> (magenta), and each catalytic site carries an iron-containing <scene name='91/917471/Cv/11'>heme group</scene> (sea-green). We compare these with the glycans identified in proteomics studies and from eighteen human MPO structures available in the PDB. | ||
Revision as of 14:38, 21 July 2022
| |||||||||||
This page complements a publication in scientific journals and is one of the Proteopedia's Interactive 3D Complement pages. For aditional details please see I3DC.
