4CC2

Complex of human Tuba C-terminal SH3 domain with human N-WASP proline- rich peptide - P212121

Summary for 4CC2

• Entry DOI: 10.2210/pdb4cc2/pdb
• Related: 4CC3 4CC4
• Descriptor: DYNAMIN-BINDING PROTEIN, NEURAL WISKOTT-ALDRICH SYNDROME PROTEIN, GLYCEROL, ... (5 entities in total)
• Functional Keywords: structural protein, src homology 3, sh3 domain, proline-rich peptide, actin cytoskeleton, cortical tension
• Biological source: HOMO SAPIENS (HUMAN); More
• Cellular location: Cytoplasm (By similarity): Q6XZF7; Cytoplasm, cytoskeleton (By similarity): O00401
• Total number of polymer chains: 4
• Total formula weight: 18231.61

Authors

Polle, L.,Rigano, L.,Julian, R.,Ireton, K.,Schubert, W.-D. (deposition date: 2013-10-17, release date: 2013-10-30, Last modification date: 2023-12-20)

Primary citation

Polle, L.,Rigano, L.A.,Julian, R.,Ireton, K.,Schubert, W.
Structural Details of Human Tuba Recruitment by Inlc of Listeria Monocytogenes Elucidate Bacterial Cell-Cell Spreading.
Structure, 22:304-, 2014

PubMed Abstract: The 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.

PubMed: 24332715
DOI: 10.1016/J.STR.2013.10.017

Experimental method

X-RAY DIFFRACTION (1.55 Å)