3NT8
Crystal Structure of Na-ASP-1
Summary for 3NT8
| Entry DOI | 10.2210/pdb3nt8/pdb |
| Related | 1CFE 1SMB 1U53 1XX5 |
| Descriptor | Ancylostoma secreted protein 1 (2 entities in total) |
| Functional Keywords | pathogenesis related-1 protein, cysteine-rich secretory protein, cap domain, immune system |
| Biological source | Necator americanus (Human hookworm) |
| Total number of polymer chains | 2 |
| Total formula weight | 91568.41 |
| Authors | Asojo, O.A. (deposition date: 2010-07-02, release date: 2011-04-27, Last modification date: 2024-11-06) |
| Primary citation | Asojo, O.A. Structure of a two-CAP-domain protein from the human hookworm parasite Necator americanus. Acta Crystallogr.,Sect.D, 67:455-462, 2011 Cited by PubMed Abstract: Major proteins secreted by the infective larval stage hookworms upon host entry include Ancylostoma secreted proteins (ASPs), which are characterized by one or two CAP (cysteine-rich secretory protein/antigen 5/pathogenesis related-1) domains. The CAP domain has been reported in diverse phylogenetically unrelated proteins, but has no confirmed function. The first structure of a two-CAP-domain protein, Na-ASP-1, from the major human hookworm parasite Necator americanus was refined to a resolution limit of 2.2 Å. The structure was solved by molecular replacement (MR) using Na-ASP-2, a one-CAP-domain ASP, as the search model. The correct MR solution could only be obtained by truncating the polyalanine model of Na-ASP-2 and removing several loops. The structure reveals two CAP domains linked by an extended loop. Overall, the carboxyl-terminal CAP domain is more similar to Na-ASP-2 than to the amino-terminal CAP domain. A large central cavity extends from the amino-terminal CAP domain to the carboxyl-terminal CAP domain, encompassing the putative CAP-binding cavity. The putative CAP-binding cavity is a characteristic cavity in the carboxyl-terminal CAP domain that contains a His and Glu pair. These residues are conserved in all single-CAP-domain proteins, but are absent in the amino-terminal CAP domain. The conserved His residues are oriented such that they appear to be capable of directly coordinating a zinc ion as observed for CAP proteins from reptile venoms. This first structure of a two-CAP-domain ASP can serve as a template for homology modeling of other two-CAP-domain proteins. PubMed: 21543848DOI: 10.1107/S0907444911008560 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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