4HHX

Structure of cytoplasmic domain of TCPE from Vibrio cholerae

Summary for 4HHX

• Entry DOI: 10.2210/pdb4hhx/pdb
• Related: 4hji
• Descriptor: Toxin coregulated pilus biosynthesis protein E, SULFATE ION (3 entities in total)
• Functional Keywords: type iv pilus assembly protein, integral inner membrane protein, gspf superfamily, polytopic membrane protein, inner membrane platform, n-terminal cytoplasmic domain, membrane protein
• Biological source: Vibrio cholerae O1 biovar El Tor str. N16961
• Cellular location: Cell inner membrane; Multi-pass membrane protein (Probable): P0C6C9
• Total number of polymer chains: 1
• Total formula weight: 13681.94

Authors

Kolappan, S.,Craig, L. (deposition date: 2012-10-10, release date: 2013-04-03, Last modification date: 2024-11-06)

Primary citation

Kolappan, S.,Craig, L.
Structure of the cytoplasmic domain of TcpE, the inner membrane core protein required for assembly of the Vibrio cholerae toxin-coregulated pilus.
Acta Crystallogr.,Sect.D, 69:513-519, 2013

PubMed Abstract: Type IV pili are long thin surface-displayed polymers of the pilin subunit that are present in a diverse group of bacteria. These multifunctional filaments are critical to virulence for pathogens such as Vibrio cholerae, which use them to form microcolonies and to secrete the colonization factor TcpF. The type IV pili are assembled from pilin subunits by a complex inner membrane machinery. The core component of the type IV pilus-assembly platform is an integral inner membrane protein belonging to the GspF superfamily of secretion proteins. These proteins somehow convert chemical energy from ATP hydrolysis by an assembly ATPase on the cytoplasmic side of the inner membrane to mechanical energy for extrusion of the growing pilus filament out of the inner membrane. Most GspF-family inner membrane core proteins are predicted to have N-terminal and central cytoplasmic domains, cyto1 and cyto2, and three transmembrane segments, TM1, TM2 and TM3. Cyto2 and TM3 represent an internal repeat of cyto1 and TM1. Here, the 1.88 Å resolution crystal structure of the cyto1 domain of V. cholerae TcpE, which is required for assembly of the toxin-coregulated pilus, is reported. This domain folds as a monomeric six-helix bundle with a positively charged membrane-interaction face at one end and a hydrophobic groove at the other end that may serve as a binding site for partner proteins in the pilus-assembly complex.

PubMed: 23519659
DOI: 10.1107/S0907444912050330

Experimental method

X-RAY DIFFRACTION (1.88 Å)