1NBW

Glycerol dehydratase reactivase

Summary for 1NBW

• Entry DOI: 10.2210/pdb1nbw/pdb
• Descriptor: GLYCEROL DEHYDRATASE REACTIVASE ALPHA SUBUNIT, GLYCEROL DEHYDRATASE REACTIVASE BETA SUBUNIT, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: glycerol dehydratase, reactivase, molecular chaperone, actin-like atpase domain, beta/beta/alpha swiveling domain, hydrolase
• Biological source: Klebsiella pneumoniae; More
• Total number of polymer chains: 4
• Total formula weight: 151391.30

Authors

Liao, D.-I.,Reiss, L.,Turner Jr., I.,Dotson, G. (deposition date: 2002-12-04, release date: 2003-01-14, Last modification date: 2024-10-16)

Primary citation

Liao, D.-I.,Reiss, L.,Turner Jr., I.,Dotson, G.
Structure of glycerol dehydratase reactivase: A new type of molecular chaperone
Structure, 11:109-119, 2003

PubMed Abstract: The function of glycerol dehydratase (GDH) reactivase is to remove damaged coenzyme B(12) from GDH that has suffered mechanism-based inactivation. The structure of GDH reactivase from Klebsiella pneumoniae was determined at 2.4 A resolution by the single isomorphous replacement with anomalous signal (SIR/AS) method. Each tetramer contains two elongated 63 kDa alpha subunits and two globular 14 kDa beta subunits. The alpha subunit contains structural features resembling both GroEL and Hsp70 groups of chaperones, and it appears chaperone like in its interactions with ATP. The fold of the beta subunit resembles that of the beta subunit of glycerol dehydratase, except that it lacks some coenzyme B(12) binding elements. A hypothesis for the reactivation mechanism of reactivase is proposed based on these structural features.

PubMed: 12517345
DOI: 10.1016/S0969-2126(02)00935-8

Experimental method

X-RAY DIFFRACTION (2.4 Å)