1Z5Y

Crystal Structure Of The Disulfide-Linked Complex Between The N-Terminal Domain Of The Electron Transfer Catalyst DsbD and The Cytochrome c Biogenesis Protein CcmG

Summary for 1Z5Y

• Entry DOI: 10.2210/pdb1z5y/pdb
• Related: 1SE1
• Descriptor: Thiol:disulfide interchange protein dsbD, Thiol:disulfide interchange protein dsbE, CHLORIDE ION, ... (5 entities in total)
• Functional Keywords: dsbd, n-terminal domain, immunoglobulin-like, ccmg, thioredoxin-like, disulfide-linked, oxidoreductase-biosynthetic protein complex, oxidoreductase/biosynthetic protein
• Biological source: Escherichia coli; More
• Cellular location: Cell inner membrane; Multi-pass membrane protein: P36655; Cell inner membrane; Single-pass membrane protein; Periplasmic side: P0AA86
• Total number of polymer chains: 2
• Total formula weight: 33421.53

Authors

Stirnimann, C.U.,Rozhkova, A.,Grauschopf, U.,Gruetter, M.G.,Glockshuber, R.,Capitani, G. (deposition date: 2005-03-21, release date: 2005-07-19, Last modification date: 2024-11-20)

Primary citation

Stirnimann, C.U.,Rozhkova, A.,Grauschopf, U.,Gruetter, M.G.,Glockshuber, R.,Capitani, G.
Structural Basis and Kinetics of DsbD-Dependent Cytochrome c Maturation
STRUCTURE, 13:985-993, 2005

PubMed Abstract: DsbD from Escherichia coli transports two electrons from cytoplasmic thioredoxin to the periplasmic substrate proteins DsbC, DsbG and CcmG. DsbD consists of an N-terminal periplasmic domain (nDsbD), a C-terminal periplasmic domain, and a central transmembrane domain. Each domain possesses two cysteines required for electron transport. Herein, we demonstrate fast (3.9 x 10(5) M(-1)s(-1)) and direct disulfide exchange between nDsbD and CcmG, a highly specific disulfide reductase essential for cytochrome c maturation. We determined the crystal structure of the disulfide-linked complex between nDsbD and the soluble part of CcmG at 1.94 A resolution. In contrast to the other two known complexes of nDsbD with target proteins, the N-terminal segment of nDsbD contributes to specific recognition of CcmG. This and other features, like the possibility of using an additional interaction surface, constitute the structural basis for the adaptability of nDsbD to different protein substrates.

PubMed: 16004871
DOI: 10.1016/j.str.2005.04.014

Experimental method

X-RAY DIFFRACTION (1.94 Å)