2D0P

Structure of diol dehydratase-reactivating factor in nucleotide free form

Summary for 2D0P

• Entry DOI: 10.2210/pdb2d0p/pdb
• Related: 2D0O
• Descriptor: diol dehydratase-reactivating factor large subunit, diol dehydratase-reactivating factor small subunit, SULFATE ION, ... (5 entities in total)
• Functional Keywords: chaperone
• Biological source: Klebsiella oxytoca; More
• Total number of polymer chains: 4
• Total formula weight: 156494.64

Authors

Shibata, N.,Mori, K.,Hieda, N.,Higuchi, Y.,Yamanishi, M.,Toraya, T. (deposition date: 2005-08-05, release date: 2006-02-28, Last modification date: 2024-03-13)

Primary citation

Shibata, N.,Mori, K.,Hieda, N.,Higuchi, Y.,Yamanishi, M.,Toraya, T.
Release of a damaged cofactor from a coenzyme B12-dependent enzyme: X-ray structures of diol dehydratase-reactivating factor
Structure, 13:1745-1754, 2005

PubMed Abstract: 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.

PubMed: 16338403
DOI: 10.1016/j.str.2005.08.011

Experimental method

X-RAY DIFFRACTION (3 Å)