Crystal structure of the N-terminal domain of the secretin GspD from ETEC determined with the assistance of a nanobody.

TitleCrystal structure of the N-terminal domain of the secretin GspD from ETEC determined with the assistance of a nanobody.
Publication TypeJournal Article
Year of Publication2009
AuthorsKorotkov, K. V., E. Pardon, J. Steyaert, and W. G. J. Hol
JournalStructure
Volume17
Issue2
Pagination255-65
Date Published2009 Feb 13
ISSN0969-2126
KeywordsAmino Acid Sequence, Crystallography, X-Ray, Enterotoxigenic Escherichia coli, Escherichia coli Proteins, Immunoglobulin Heavy Chains, Models, Biological, Models, Molecular, Molecular Sequence Data, Porins, Protein Binding, Protein Multimerization, Protein Structure, Quaternary, Protein Structure, Secondary, Protein Structure, Tertiary, Secretin, Sequence Homology, Amino Acid
Abstract

Secretins are among the largest bacterial outer membrane proteins known. Here we report the crystal structure of the periplasmic N-terminal domain of GspD (peri-GspD) from the type 2 secretion system (T2SS) secretin in complex with a nanobody, the VHH domain of a heavy-chain camelid antibody. Two different crystal forms contained the same compact peri-GspD:nanobody heterotetramer. The nanobody contacts peri-GspD mainly via CDR3 and framework residues. The peri-GspD structure reveals three subdomains, with the second and third subdomains exhibiting the KH fold which also occurs in ring-forming proteins of the type 3 secretion system. The first subdomain of GspD is related to domains in phage tail proteins and outer membrane TonB-dependent receptors. A dodecameric peri-GspD model is proposed in which a solvent-accessible beta strand of the first subdomain interacts with secreted proteins and/or T2SS partner proteins by beta strand complementation.

DOI10.1016/j.str.2008.11.011
Alternate JournalStructure
PubMed ID19217396
PubMed Central IDPMC2662362
Grant ListAI34501 / AI / NIAID NIH HHS / United States
R01 AI034501-15 / AI / NIAID NIH HHS / United States