1pm9

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[[Image:1pm9.jpg|left|200px]]
[[Image:1pm9.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1pm9 |SIZE=350|CAPTION= <scene name='initialview01'>1pm9</scene>, resolution 1.70&Aring;
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The line below this paragraph, containing "STRUCTURE_1pm9", 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=MN3:MANGANESE+(III)+ION'>MN3</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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|DOMAIN=
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{{STRUCTURE_1pm9| PDB=1pm9 | SCENE= }}
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|RELATEDENTRY=[[1pl4|1PL4]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pm9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pm9 OCA], [http://www.ebi.ac.uk/pdbsum/1pm9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1pm9 RCSB]</span>
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}}
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'''CRYSTAL STRUCTURE OF HUMAN MNSOD H30N, Y166F MUTANT'''
'''CRYSTAL STRUCTURE OF HUMAN MNSOD H30N, Y166F MUTANT'''
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[[Category: Fan, L.]]
[[Category: Fan, L.]]
[[Category: Tainer, J A.]]
[[Category: Tainer, J A.]]
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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 05:14:40 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:01:33 2008''
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Revision as of 02:14, 3 May 2008

Image:1pm9.jpg

Template:STRUCTURE 1pm9

CRYSTAL STRUCTURE OF HUMAN MNSOD H30N, Y166F MUTANT


Overview

The side chains of His30 and Tyr166 from adjacent subunits in the homotetramer human manganese superoxide dismutase (Mn-SOD) form a hydrogen bond across the dimer interface and participate in a hydrogen-bonded network that extends to the active site. Compared with wild-type Mn-SOD, the site-specific mutants H30N, Y166F, and the corresponding double mutant showed 10-fold decreases in steady-state constants for catalysis measured by pulse radiolysis. The observation of no additional effect upon the second mutation is an example of cooperatively interacting residues. A similar effect was observed in the thermal stability of these enzymes; the double mutant did not reduce the major unfolding transition to an extent greater than either single mutant. The crystal structures of these site-specific mutants each have unique conformational changes, but each has lost the hydrogen bond across the dimer interface, which results in a decrease in catalysis. These same mutations caused an enhancement of the dissociation of the product-inhibited complex. That is, His30 and Tyr166 in wild-type Mn-SOD act to prolong the lifetime of the inhibited complex. This would have a selective advantage in blocking a cellular overproduction of toxic H2O2.

About this Structure

1PM9 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Amino acid substitution at the dimeric interface of human manganese superoxide dismutase., Hearn AS, Fan L, Lepock JR, Luba JP, Greenleaf WB, Cabelli DE, Tainer JA, Nick HS, Silverman DN, J Biol Chem. 2004 Feb 13;279(7):5861-6. Epub 2003 Nov 24. PMID:14638684 Page seeded by OCA on Sat May 3 05:14:40 2008

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