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| - | [[Image:2adp.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2adp| PDB=2adp | SCENE= }} | | {{STRUCTURE_2adp| PDB=2adp | SCENE= }} |
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| - | '''Nitrated Human Manganese Superoxide Dismutase'''
| + | ===Nitrated Human Manganese Superoxide Dismutase=== |
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| - | ==Overview==
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| - | A cellular consequence of the reaction of superoxide and nitric oxide is enhanced peroxynitrite levels. Reaction of peroxynitrite with manganese superoxide dismutase (MnSOD) causes nitration of the active-site residue Tyr34 and nearly complete inhibition of catalysis. We report the crystal structures at 2.4 A resolution of human MnSOD nitrated by peroxynitrite and the unmodified MnSOD. A comparison of these structures showed no significant conformational changes of active-site residues or solvent displacement. The side chain of 3-nitrotyrosine 34 had a single conformation that extended toward the manganese with O1 of the nitro group within hydrogen-bonding distance (3.1 A) of Nepsilon2 of the second-shell ligand Gln143. Also, nitration of Tyr34 caused a weakening, as evidenced by the lengthening, of a hydrogen bond between its phenolic OH and Gln143, part of an extensive hydrogen-bond network in the active site. Inhibition of catalysis can be attributed to a steric effect of 3-nitrotyrosine 34 that impedes substrate access and binding, and alteration of the hydrogen-bond network that supports proton transfer in catalysis. It is also possible that an electrostatic effect of the nitro group has altered the finely tuned redox potential necessary for efficient catalysis, although the redox potential of nitrated MnSOD has not been measured.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_16443160}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16443160 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_16443160}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Silverman, D N.]] | | [[Category: Silverman, D N.]] |
| | [[Category: Oxidoreductase]] | | [[Category: Oxidoreductase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:55:00 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 17:48:55 2008'' |
Revision as of 14:48, 28 July 2008
Template:STRUCTURE 2adp
Nitrated Human Manganese Superoxide Dismutase
Template:ABSTRACT PUBMED 16443160
About this Structure
2ADP is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of nitrated human manganese superoxide dismutase: mechanism of inactivation., Quint P, Reutzel R, Mikulski R, McKenna R, Silverman DN, Free Radic Biol Med. 2006 Feb 1;40(3):453-8. Epub 2005 Nov 9. PMID:16443160
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