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 DOI | 10.2210/pdb3ezj/pdb |
Descriptor | General secretion pathway protein GspD, NANOBODY NBGSPD_7, PHOSPHATE ION, ... (5 entities in total) |
Functional Keywords | general secretory pathway, secretin, single chain antibody, protein transport, immune system, complex |
Biological source | Escherichia coli More |
Total number of polymer chains | 8 |
Total formula weight | 160804.99 |
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 citation | Korotkov, 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: 19217396DOI: 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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