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2Y8R

Crystal structure of apo AMA1 mutant (Tyr230Ala) from Toxoplasma gondii

Summary for 2Y8R
Entry DOI10.2210/pdb2y8r/pdb
Related2Y8S 2Y8T
DescriptorAPICAL MEMBRANE ANTIGEN, PUTATIVE, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
Functional Keywordsmembrane protein, moving junction, invasion
Biological sourceTOXOPLASMA GONDII
Total number of polymer chains4
Total formula weight192570.28
Authors
Tonkin, M.L.,Roques, M.,Lamarque, M.H.,Pugniere, M.,Douguet, D.,Crawford, J.,Lebrun, M.,Boulanger, M.J. (deposition date: 2011-02-10, release date: 2011-08-03, Last modification date: 2020-07-29)
Primary citationTonkin, M.L.,Roques, M.,Lamarque, M.H.,Pugniere, M.,Douguet, D.,Crawford, J.,Lebrun, M.,Boulanger, M.J.
Host Cell Invasion by Apicomplexan Parasites: Insights from the Co-Structure of Ama1 with a Ron2 Peptide
Science, 333:463-, 2011
Cited by
PubMed Abstract: Apicomplexan parasites such as Toxoplasma gondii and Plasmodium species actively invade host cells through a moving junction (MJ) complex assembled at the parasite-host cell interface. MJ assembly is initiated by injection of parasite rhoptry neck proteins (RONs) into the host cell, where RON2 spans the membrane and functions as a receptor for apical membrane antigen 1 (AMA1) on the parasite. We have determined the structure of TgAMA1 complexed with a RON2 peptide at 1.95 angstrom resolution. A stepwise assembly mechanism results in an extensive buried surface area, enabling the MJ complex to resist the mechanical forces encountered during host cell invasion. Besides providing insights into host cell invasion by apicomplexan parasites, the structure offers a basis for designing therapeutics targeting these global pathogens.
PubMed: 21778402
DOI: 10.1126/SCIENCE.1204988
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.45 Å)
Structure validation

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