1S9U

Atomic structure of a putative anaerobic dehydrogenase component

Summary for 1S9U

• Entry DOI: 10.2210/pdb1s9u/pdb
• Descriptor: putative component of anaerobic dehydrogenases, SULFATE ION, DI(HYDROXYETHYL)ETHER, ... (4 entities in total)
• Functional Keywords: structural genomics, anaerobic dehydrogenases component, psi, protein structure initiative, midwest center for structural genomics, mcsg, unknown function
• Biological source: Salmonella typhimurium
• Total number of polymer chains: 1
• Total formula weight: 24698.16

Authors

Qiu, Y.,Zhang, R.,Tereshko, V.,Kim, Y.,Collart, F.,Joachimiak, A.,Kossiakoff, A.,Midwest Center for Structural Genomics (MCSG) (deposition date: 2004-02-05, release date: 2004-06-08, Last modification date: 2011-07-13)

Primary citation

Qiu, Y.,Zhang, R.,Binkowski, T.A.,Tereshko, V.,Joachimiak, A.,Kossiakoff, A.
The 1.38 A crystal structure of DmsD protein from Salmonella typhimurium, a proofreading chaperone on the Tat pathway.
Proteins, 71:525-533, 2008

PubMed Abstract: The DmsD protein is necessary for the biogenesis of dimethyl sulphoxide (DMSO) reductase in many prokaryotes. It performs a critical chaperone function initiated through its binding to the twin-arginine signal peptide of DmsA, the catalytic subunit of DMSO reductase. Upon binding to DmsD, DmsA is translocated to the periplasm via the so-called twin-arginine translocation (Tat) pathway. Here we report the 1.38 A crystal structure of the protein DmsD from Salmonella typhimurium and compare it with a close functional homolog, TorD. DmsD has an all-alpha fold structure with a notable helical extension located at its N-terminus with two solvent exposed hydrophobic residues. A major difference between DmsD and TorD is that TorD structure is a domain-swapped dimer, while DmsD exists as a monomer. Nevertheless, these two proteins have a number of common features suggesting they function by using similar mechanisms. A possible signal peptide-binding site is proposed based on structural similarities. Computational analysis was used to identify a potential GTP binding pocket on similar surfaces of DmsD and TorD structures.

PubMed: 18175314
DOI: 10.1002/prot.21828

Experimental method

X-RAY DIFFRACTION (1.38 Å)