1gv3

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File:1gv3.gif


1gv3, resolution 2.00Å

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THE 2.0 ANGSTROM RESOLUTION STRUCTURE OF THE CATALYTIC PORTION OF A CYANOBACTERIAL MEMBRANE-BOUND MANGANESE SUPEROXIDE DISMUTASE

OverviewOverview

Cyanobacteria are shown to be unique in containing membrane-bound, manganese superoxide dismutases (MnSOD). They are homodimeric type 2, membrane proteins that protect this phototrophic organism against, oxidative stress. We have determined, for the first time, the 2.0A, resolution structure of the catalytic portion of the MnSOD from the, filamentous cyanobacterium Anabaena PCC 7120. Within each subunit, both, the N-terminal helical hairpin (His94 and His145) and the C-terminal, alpha/beta domain (His232 and Asp228) contribute ligands to the catalytic, manganese site. Together with a water or hydroxide ion (OH(x)) a, five-coordinated trigonal bipyramidal geometry is formed, with OH(x) and, His90 forming the axial ligands and manganese shifted out of the, equatorial plane in the direction ... [(full description)]

About this StructureAbout this Structure

1GV3 is a [Single protein] structure of sequence from [Anabaena sp.] with MN as [ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

ReferenceReference

The 2.0A resolution structure of the catalytic portion of a cyanobacterial membrane-bound manganese superoxide dismutase., Atzenhofer W, Regelsberger G, Jacob U, Peschek G, Furtmuller P, Huber R, Obinger C, J Mol Biol. 2002 Aug 16;321(3):479-89. PMID:12162960

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