2d0o

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Revision as of 16:52, 29 January 2008

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spinqualitylabelsall models 2d0o, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Strcuture of diol dehydratase-reactivating factor complexed with ADP and Mg2+

Overview

The crystal structures of ADP bound and nucleotide-free forms of molecular, chaperone-like diol dehydratase-reactivating factor (DDR) were determined, at 2.0 and 3.0 A, respectively. DDR exists as a dimer of heterodimer, (alphabeta)2. The alpha subunit has four domains: ATPase domain, swiveling, domain, linker domain, and insert domain. The beta subunit, composed of a, single domain, has a similar fold to the beta subunit of diol dehydratase, (DD). The binding of an ADP molecule to the nucleotide binding site of DDR, causes a marked conformational change of the ATPase domain of the alpha, subunit, which would weaken the interactions between the DDR alpha and, beta subunits and make the displacement of the DDR beta subunit by DD, through the beta subunit possible. The binding of the DD beta subunit to, the DDR alpha subunit induces steric repulsion between the DDR alpha and, DD alpha subunits that would lead to the release of a damaged cofactor, from inactivated holoDD.

About this Structure

2D0O is a Protein complex structure of sequences from Klebsiella oxytoca with , and as ligands. Full crystallographic information is available from OCA.

Reference

Release of a damaged cofactor from a coenzyme B12-dependent enzyme: X-ray structures of diol dehydratase-reactivating factor., Shibata N, Mori K, Hieda N, Higuchi Y, Yamanishi M, Toraya T, Structure. 2005 Dec;13(12):1745-54. PMID:16338403

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