3FM8
Crystal structure of full length centaurin alpha-1 bound with the FHA domain of KIF13B (CAPRI target)
Summary for 3FM8
| Entry DOI | 10.2210/pdb3fm8/pdb |
| Descriptor | Kinesin-like protein KIF13B, Centaurin-alpha-1, UNKNOWN ATOM OR ION, ... (6 entities in total) |
| Functional Keywords | kinesin, gap, gtpase activation, structural genomics consortium, sgc, atp-binding, cytoskeleton, microtubule, motor protein, nucleotide-binding, phosphoprotein, metal-binding, nucleus, zinc-finger, metal binding protein, transport protein-hydrolase activator complex, transport protein/hydrolase activator |
| Biological source | Homo sapiens (human) More |
| Cellular location | Cytoplasm, cytoskeleton : Q9NQT8 Nucleus: O75689 |
| Total number of polymer chains | 4 |
| Total formula weight | 119749.97 |
| Authors | Shen, L.,Tong, Y.,Tempel, W.,MacKenzie, F.,Arrowsmith, C.H.,Edwards, A.M.,Bountra, C.,Weigelt, J.,Bochkarev, A.,Park, H.,Structural Genomics Consortium (SGC) (deposition date: 2008-12-19, release date: 2009-08-25, Last modification date: 2024-04-03) |
| Primary citation | Tong, Y.,Tempel, W.,Wang, H.,Yamada, K.,Shen, L.,Senisterra, G.A.,MacKenzie, F.,Chishti, A.H.,Park, H.W. Phosphorylation-independent dual-site binding of the FHA domain of KIF13 mediates phosphoinositide transport via centaurin alpha1. Proc.Natl.Acad.Sci.USA, 107:20346-20351, 2010 Cited by PubMed Abstract: Phosphatidylinositol 3,4,5-triphosphate (PIP3) plays a key role in neuronal polarization and axon formation. PIP3-containing vesicles are transported to axon tips by the kinesin KIF13B via an adaptor protein, centaurin α1 (CENTA1). KIF13B interacts with CENTA1 through its forkhead-associated (FHA) domain. We solved the crystal structures of CENTA1 in ligand-free, KIF13B-FHA domain-bound, and PIP3 head group (IP4)-bound conformations, and the CENTA1/KIF13B-FHA/IP4 ternary complex. The first pleckstrin homology (PH) domain of CENTA1 specifically binds to PIP3, while the second binds to both PIP3 and phosphatidylinositol 3,4-biphosphate (PI(3,4)P(2)). The FHA domain of KIF13B interacts with the PH1 domain of one CENTA1 molecule and the ArfGAP domain of a second CENTA1 molecule in a threonine phosphorylation-independent fashion. We propose that full-length KIF13B and CENTA1 form heterotetramers that can bind four phosphoinositide molecules in the vesicle and transport it along the microtubule. PubMed: 21057110DOI: 10.1073/pnas.1009008107 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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