2YKT

Crystal structure of the I-BAR domain of IRSp53 (BAIAP2) in complex with an EHEC derived Tir peptide

Summary for 2YKT

• Entry DOI: 10.2210/pdb2ykt/pdb
• Related: 1WDZ 1Y2O
• Descriptor: BRAIN-SPECIFIC ANGIOGENESIS INHIBITOR 1-ASSOCIATED PROTEIN 2, TRANSLOCATED INTIMIN RECEPTOR PROTEIN, SULFATE ION, ... (4 entities in total)
• Functional Keywords: signaling protein, npy motif, binding pocket
• Biological source: HOMO SAPIENS (HUMAN); More
• Cellular location: Cytoplasm: Q9UQB8
• Total number of polymer chains: 2
• Total formula weight: 30237.31

Authors

de Groot, J.C.,Schlueter, K.,Carius, Y.,Quedenau, C.,Vingadassalom, D.,Faix, J.,Weiss, S.M.,Reichelt, J.,Standfuss-Gabisch, C.,Lesser, C.F.,Leong, J.M.,Heinz, D.W.,Buessow, K.,Stradal, T.E.B. (deposition date: 2011-05-30, release date: 2011-09-07, Last modification date: 2024-10-23)

Primary citation

De Groot, J.C.,Schluter, K.,Carius, Y.,Quedenau, C.,Vingadassalom, D.,Faix, J.,Weiss, S.M.,Reichelt, J.,Standfuss-Gabisch, C.,Lesser, C.F.,Leong, J.M.,Heinz, D.W.,Bussow, K.,Stradal, T.E.B.
Structural Basis for Complex Formation between Human Irsp53 and the Translocated Intimin Receptor Tir of Enterohemorrhagic E. Coli.
Structure, 19:1294-, 2011

PubMed Abstract: Actin assembly beneath enterohemorrhagic E. coli (EHEC) attached to its host cell is triggered by the intracellular interaction of its translocated effector proteins Tir and EspF(U) with human IRSp53 family proteins and N-WASP. Here, we report the structure of the N-terminal I-BAR domain of IRSp53 in complex with a Tir-derived peptide, in which the homodimeric I-BAR domain binds two Tir molecules aligned in parallel. This arrangement provides a protein scaffold linking the bacterium to the host cell's actin polymerization machinery. The structure uncovers a specific peptide-binding site on the I-BAR surface, conserved between IRSp53 and IRTKS. The Tir Asn-Pro-Tyr (NPY) motif, essential for pedestal formation, is specifically recognized by this binding site. The site was confirmed by mutagenesis and in vivo-binding assays. It is possible that IRSp53 utilizes the NPY-binding site for additional interactions with as yet unknown partners within the host cell.

PubMed: 21893288
DOI: 10.1016/J.STR.2011.06.015

Experimental method

X-RAY DIFFRACTION (2.11 Å)