1aop

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spinqualitylabelsall models 1aop, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

SULFITE REDUCTASE STRUCTURE AT 1.6 ANGSTROM RESOLUTION

Overview

Fundamental chemical transformations for biogeochemical cycling of sulfur, and nitrogen are catalyzed by sulfite and nitrite reductases. The, crystallographic structure of Escherichia coli sulfite reductase, hemoprotein (SiRHP), which catalyzes the concerted six-electron reductions, of sulfite to sulfide and nitrite to ammonia, was solved with, multiwavelength anomalous diffraction (MAD) of the native siroheme and, Fe4S4 cluster cofactors, multiple isomorphous replacement, and, selenomethionine sequence markers. Twofold symmetry within the, 64-kilodalton polypeptide generates a distinctive three-domain alpha/beta, fold that controls cofactor assembly and reactivity. Homology regions, conserved between the symmetry-related halves of SiRHP and among other, sulfite and nitrite reductases ... [(full description)]

About this Structure

1AOP is a [Single protein] structure of sequence from [Escherichia coli] with PO4, K, SF4 and SRM as [ligands]. This structure superseeds the now removed PDB entry 1GEO. Active as [[1]], with EC number [1.8.1.2]. Full crystallographic information is available from [OCA].

Reference

Sulfite reductase structure at 1.6 A: evolution and catalysis for reduction of inorganic anions., Crane BR, Siegel LM, Getzoff ED, Science. 1995 Oct 6;270(5233):59-67. PMID:7569952[[Category: [4fe-4s]]]

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