1q0e: Difference between revisions
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==Atomic resolution (1.15 ) crystal structure of bovine copper, zinc superoxide dismutase== | ==Atomic resolution (1.15 ) crystal structure of bovine copper, zinc superoxide dismutase== | ||
<StructureSection load='1q0e' size='340' side='right' caption='[[1q0e]], [[Resolution|resolution]] 1.15Å' scene=''> | <StructureSection load='1q0e' size='340' side='right'caption='[[1q0e]], [[Resolution|resolution]] 1.15Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1q0e]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q0E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Q0E FirstGlance]. <br> | <table><tr><td colspan='2'>[[1q0e]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q0E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Q0E FirstGlance]. <br> | ||
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</div> | </div> | ||
<div class="pdbe-citations 1q0e" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1q0e" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Superoxide Dismutase|Superoxide Dismutase]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Large Structures]] | |||
[[Category: Superoxide dismutase]] | [[Category: Superoxide dismutase]] | ||
[[Category: Hasnain, S S]] | [[Category: Hasnain, S S]] | ||
Revision as of 13:22, 27 November 2019
Atomic resolution (1.15 ) crystal structure of bovine copper, zinc superoxide dismutaseAtomic resolution (1.15 ) crystal structure of bovine copper, zinc superoxide dismutase
Structural highlights
Function[SODC_BOVIN] Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedCopper zinc superoxide dismutase (CuZnSOD) forms a crucial component of the cellular response to oxidative stress by catalyzing the dismutation of the superoxide radical to hydrogen peroxide and water. Mutations in human CuZnSOD are associated with the development of familial amyotrophic lateral sclerosis (motor neuron disease). We have determined the structure of fully reduced bovine CuZnSOD to 1.15 A, the only atomic resolution structure for an intact CuZnSOD and one of only a small number for metalloproteins. For the first time, both subunits have been captured with the three coordinate Cu(I) ligation required by the generally accepted catalytic mechanism, where dismutation of the superoxide radical occurs via reduction of Cu. Furthermore, the improved resolution compared to previous studies (to 1.65 A) has allowed a more detailed examination of the metal center environment and its associated water network in the active site channel, facilitating the analysis of potential proton transfer routes. Structure of fully reduced bovine copper zinc superoxide dismutase at 1.15 A.,Hough MA, Hasnain SS Structure. 2003 Aug;11(8):937-46. PMID:12906825[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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