Entry | Database: PDB / ID: 7s5u |
---|
Title | Extended bipolar assembly domain of kinesin-5 minifilament |
---|
Components | Kinesin-like protein Klp61F |
---|
Keywords | CELL CYCLE / Kinesin-5 / Bipolar assembly / four-helical-bundle |
---|
Function / homology | Function and homology information
aster / plus-end directed microtubule sliding / fusome organization / fusome / COPI-dependent Golgi-to-ER retrograde traffic / Kinesins / centrosome separation / spindle elongation / mitotic spindle microtubule / microtubule bundle formation ...aster / plus-end directed microtubule sliding / fusome organization / fusome / COPI-dependent Golgi-to-ER retrograde traffic / Kinesins / centrosome separation / spindle elongation / mitotic spindle microtubule / microtubule bundle formation / plus-end-directed microtubule motor activity / positive regulation of Golgi to plasma membrane protein transport / mitotic centrosome separation / kinesin complex / microtubule associated complex / microtubule-based movement / mitotic spindle pole / Golgi organization / cytoskeletal motor activity / protein secretion / mitotic spindle assembly / mitotic spindle organization / spindle microtubule / spindle / mitotic spindle / mitotic cell cycle / microtubule binding / microtubule / cell division / endoplasmic reticulum / Golgi apparatus / ATP binding / nucleus / cytoplasmSimilarity search - Function Kinesin-associated microtubule-binding domain / Kinesin-associated microtubule-binding / : / : / Kinesin motor domain signature. / Kinesin motor domain, conserved site / Kinesin motor domain / Kinesin motor domain profile. / Kinesin motor, catalytic domain. ATPase. / Kinesin motor domain ...Kinesin-associated microtubule-binding domain / Kinesin-associated microtubule-binding / : / : / Kinesin motor domain signature. / Kinesin motor domain, conserved site / Kinesin motor domain / Kinesin motor domain profile. / Kinesin motor, catalytic domain. ATPase. / Kinesin motor domain / Kinesin motor domain superfamily / P-loop containing nucleoside triphosphate hydrolaseSimilarity search - Domain/homology |
---|
Biological species |  Drosophila melanogaster (fruit fly) |
---|
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 4.41 Å |
---|
Authors | Nithianantham, S. / Al-Bassam, J. |
---|
Funding support | United States, 2items Organization | Grant number | Country |
---|
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS) | GM110283 | United States | National Science Foundation (NSF, United States) | 1615991 | United States |
|
---|
Citation | Journal: Mol.Biol.Cell / Year: 2023 Title: The kinesin-5 tail and bipolar miniflament domains are the origin of its microtubule crosslinking and sliding activity. Authors: Nithianantham, S. / Iwanski, M.K. / Gaska, I. / Pandey, H. / Bodrug, T. / Inagaki, S. / Major, J. / Brouhard, G.J. / Gheber, L. / Rosenfeld, S.S. / Forth, S. / Hendricks, A.G. / Al-Bassam, J. |
---|
History | Deposition | Sep 12, 2021 | Deposition site: RCSB / Processing site: RCSB |
---|
Revision 1.0 | Mar 15, 2023 | Provider: repository / Type: Initial release |
---|
Revision 1.1 | Sep 6, 2023 | Group: Data collection / Database references / Refinement description Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / citation / citation_author / struct_ncs_dom_lim Item: _citation.journal_abbrev / _citation.journal_id_CSD ..._citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id |
---|
Revision 1.2 | Oct 25, 2023 | Group: Refinement description / Category: pdbx_initial_refinement_model |
---|
|
---|