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| {{STRUCTURE_1pl4| PDB=1pl4 | SCENE= }} | | {{STRUCTURE_1pl4| PDB=1pl4 | SCENE= }} |
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| '''Crystal Structure of human MnSOD Y166F mutant'''
| | ===Crystal Structure of human MnSOD Y166F mutant=== |
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| ==Overview==
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| 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. | | The line below this paragraph, {{ABSTRACT_PUBMED_14638684}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 14638684 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_14638684}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Tainer, J A.]] | | [[Category: Tainer, J A.]] |
| [[Category: Oxidoreductase]] | | [[Category: Oxidoreductase]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:12:44 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 12:05:34 2008'' |
