1e60

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spinqualitylabelsall models 1e60, resolution 2.0Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

OXIDIZED DMSO REDUCTASE EXPOSED TO HEPES-STRUCTURE II BUFFER

Overview

Much is unknown concerning the role of thiolate ligands of molybdenum in, molybdopterin enzymes. It has been suggested that thiolate dissociation, from molybdenum is part of the catalytic mechanism of bis-molybdopterin, enzymes of the dimethyl sulfoxide reductase (DMSOR) family. For DMSOR from, Rhodobacter capsulatus, thiolate dissociation has therefore been, investigated crystallographically, by UV/visible spectroscopy, and by, enzyme assays. When crystallized from sodium citrate, all four thiolates, of DMSOR are within bonding distance of Mo, but after extended exposure to, Na(+)-Hepes, a pair of thiolates dissociates, a mixture of structures, being indicated after shorter exposures to this buffer. DMSOR is stable in, sodium citrate and other buffers but unstable aerobically although ... [(full description)]

About this Structure

1E60 is a [Single protein] structure of sequence from [Rhodobacter capsulatus] with SO4, PGD and 2MO as [ligands]. Structure known Active Sites: MOA and MOC. Full crystallographic information is available from [OCA].

Reference

Reversible dissociation of thiolate ligands from molybdenum in an enzyme of the dimethyl sulfoxide reductase family., Bray RC, Adams B, Smith AT, Bennett B, Bailey S, Biochemistry. 2000 Sep 19;39(37):11258-69. PMID:10985771

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