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3EZJ

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

Summary for 3EZJ
Entry DOI10.2210/pdb3ezj/pdb
DescriptorGeneral secretion pathway protein GspD, NANOBODY NBGSPD_7, PHOSPHATE ION, ... (5 entities in total)
Functional Keywordsgeneral secretory pathway, secretin, single chain antibody, protein transport, immune system, complex
Biological sourceEscherichia coli
More
Total number of polymer chains8
Total formula weight160804.99
Authors
Korotkov, K.V.,Pardon, E.,Steyaert, J.,Hol, W.G. (deposition date: 2008-10-22, release date: 2009-02-17, Last modification date: 2024-10-30)
Primary citationKorotkov, K.V.,Pardon, E.,Steyaert, J.,Hol, W.G.
Crystal structure of the N-terminal domain of the secretin GspD from ETEC determined with the assistance of a nanobody.
Structure, 17:255-265, 2009
Cited by
PubMed 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.
PubMed: 19217396
DOI: 10.1016/j.str.2008.11.011
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.8 Å)
Structure validation

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