2adp

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[[Image:2adp.gif|left|200px]]
[[Image:2adp.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 2adp |SIZE=350|CAPTION= <scene name='initialview01'>2adp</scene>, resolution 2.4&Aring;
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The line below this paragraph, containing "STRUCTURE_2adp", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NIY:META-NITRO-TYROSINE'>NIY</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.1 1.15.1.1] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= SOD2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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-->
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|DOMAIN=
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{{STRUCTURE_2adp| PDB=2adp | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2adp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2adp OCA], [http://www.ebi.ac.uk/pdbsum/2adp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2adp RCSB]</span>
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}}
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'''Nitrated Human Manganese Superoxide Dismutase'''
'''Nitrated Human Manganese Superoxide Dismutase'''
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[[Category: Reutzel, R.]]
[[Category: Reutzel, R.]]
[[Category: Silverman, D N.]]
[[Category: Silverman, D N.]]
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[[Category: oxidoreductase]]
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[[Category: Oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:55:00 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:51:13 2008''
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Revision as of 15:55, 3 May 2008

Template:STRUCTURE 2adp

Nitrated Human Manganese Superoxide Dismutase


Overview

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.

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 Page seeded by OCA on Sat May 3 18:55:00 2008

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