4cc3
Complex of human Tuba C-terminal SH3 domain and Mena proline-rich peptide - H3Complex of human Tuba C-terminal SH3 domain and Mena proline-rich peptide - H3
Structural highlights
FunctionDNMBP_HUMAN Scaffold protein that links dynamin with actin-regulating proteins. May play a role in membrane trafficking between the cell surface and the Golgi (By similarity). Publication Abstract from PubMedThe human pathogen Listeria monocytogenes is able to directly spread to neighboring cells of host tissues, a process recently linked to the virulence factor InlC. InlC targets the sixth SH3 domain (SH3-6) of human Tuba, disrupting its physiological interaction with the cytoskeletal protein N-WASP. The resulting loss of cortical actin tension may slacken the junctional membrane, allowing protrusion formation by motile Listeria. Complexes of Tuba SH3-6 with physiological partners N-WASP and Mena reveal equivalent binding modes but distinct affinities. The interaction surface of the infection complex InlC/Tuba SH3-6 is centered on phenylalanine 146 of InlC stacking upon asparagine 1569 of Tuba. Replacing Phe146 by alanine largely abrogates molecular affinity and in vivo mimics deletion of inlC. Collectively, our findings indicate that InlC hijacks Tuba through its LRR domain, blocking the peptide binding groove to prevent recruitment of its physiological partners. Structural Details of Human Tuba Recruitment by InlC of Listeria monocytogenes Elucidate Bacterial Cell-Cell Spreading.,Polle L, Rigano LA, Julian R, Ireton K, Schubert WD Structure. 2013 Dec 10. pii: S0969-2126(13)00429-2. doi:, 10.1016/j.str.2013.10.017. PMID:24332715[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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