Entry | Database: PDB / ID: 5jvd |
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Title | Tubulin-TUB092 complex |
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Components | - (Tubulin beta-2B ...) x 2
- Stathmin-4
- Tubulin alpha-1B chain
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Keywords | CELL CYCLE / TUBULIN FOLD / CYTOSKELETON / MICROTUBULE |
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Function / homology | Function and homology information
tubulin-tyrosine ligase activity / positive regulation of axon guidance / microtubule depolymerization / regulation of microtubule polymerization or depolymerization / microtubule-based process / cytoplasmic microtubule / tubulin binding / cellular response to interleukin-4 / spindle microtubule / protein modification process ...tubulin-tyrosine ligase activity / positive regulation of axon guidance / microtubule depolymerization / regulation of microtubule polymerization or depolymerization / microtubule-based process / cytoplasmic microtubule / tubulin binding / cellular response to interleukin-4 / spindle microtubule / protein modification process / structural constituent of cytoskeleton / microtubule cytoskeleton organization / neuron migration / neuron projection development / mitotic cell cycle / double-stranded RNA binding / microtubule cytoskeleton / growth cone / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / microtubule / neuron projection / cilium / protein heterodimerization activity / nucleotide binding / GTPase activity / ubiquitin protein ligase binding / GTP binding / Golgi apparatus / metal ion binding / cytosol / cytoplasmSimilarity search - Function Methane Monooxygenase Hydroxylase; Chain G, domain 1 - #30 / Methane Monooxygenase Hydroxylase; Chain G, domain 1 / Rossmann fold - #11480 / Tubulin-tyrosine ligase/Tubulin polyglutamylase / Tubulin-tyrosine ligase family / TTL domain profile. / Helix hairpin bin / Stathmin family / Stathmin, conserved site / Stathmin superfamily ...Methane Monooxygenase Hydroxylase; Chain G, domain 1 - #30 / Methane Monooxygenase Hydroxylase; Chain G, domain 1 / Rossmann fold - #11480 / Tubulin-tyrosine ligase/Tubulin polyglutamylase / Tubulin-tyrosine ligase family / TTL domain profile. / Helix hairpin bin / Stathmin family / Stathmin, conserved site / Stathmin superfamily / Stathmin family / Stathmin family signature 1. / Stathmin family signature 2. / Stathmin-like (SLD) domain profile. / ATP-grasp fold, A domain / Tubulin/FtsZ, C-terminal domain / Tubulin/FtsZ, GTPase domain / ATP-grasp fold, B domain / D-amino Acid Aminotransferase; Chain A, domain 1 / 60s Ribosomal Protein L30; Chain: A; / Tubulin-beta mRNA autoregulation signal. / Alpha tubulin / Beta tubulin, autoregulation binding site / Beta tubulin / Tubulin / Tubulin, C-terminal / Tubulin C-terminal domain / Tubulin, conserved site / Tubulin subunits alpha, beta, and gamma signature. / Tubulin/FtsZ family, C-terminal domain / Tubulin/FtsZ-like, C-terminal domain / Tubulin/FtsZ, C-terminal / Tubulin/FtsZ, 2-layer sandwich domain / Dna Ligase; domain 1 / Tubulin/FtsZ family, GTPase domain / Tubulin/FtsZ family, GTPase domain / Tubulin/FtsZ, GTPase domain / Tubulin/FtsZ, GTPase domain superfamily / Helix non-globular / Special / Helix Hairpins / Rossmann fold / 2-Layer Sandwich / Orthogonal Bundle / 3-Layer(aba) Sandwich / Mainly Alpha / Alpha BetaSimilarity search - Domain/homology Chem-6NL / PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER / GUANOSINE-5'-DIPHOSPHATE / GUANOSINE-5'-TRIPHOSPHATE / Tubulin tyrosine ligase / Stathmin-4 / Tubulin alpha-1B chain / Tubulin beta-2B chainSimilarity search - Component |
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Biological species |  Rattus norvegicus (Norway rat)
 Gallus gallus (chicken)
 Bos taurus (domestic cattle) |
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Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2.393 Å |
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Authors | Canela, M.-D. / Noppen, S. / Bueno, O. / Prota, A.E. / Bargsten, K. / Saez-Calvo, G. / Jimeno, M.-L. / Benkheil, M. / Ribatti, D. / Velazquez, S. ...Canela, M.-D. / Noppen, S. / Bueno, O. / Prota, A.E. / Bargsten, K. / Saez-Calvo, G. / Jimeno, M.-L. / Benkheil, M. / Ribatti, D. / Velazquez, S. / Camarasa, M.-J. / Diaz, J.F. / Steinmetz, M.O. / Priego, E.-M. / Perez-Perez, M.-J. / Liekens, S. |
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Funding support | Spain, Switzerland, 4items Organization | Grant number | Country |
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Spanish Ministry of Economy and Competitiveness | SAF2012- 39760-C02-01 | Spain | Spanish Ministry of Economy and Competitiveness | BIO2013-42984-R | Spain | Comunidad de Madrid | BIPEDD2; ref. P2010/BMD-2457 | Spain | Swiss National Science Foundation | 310030B_138659 and 31003A_166608 | Switzerland |
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Citation | Journal: Oncotarget / Year: 2017 Title: Antivascular and antitumor properties of the tubulin-binding chalcone TUB091. Authors: Canela, M.D. / Noppen, S. / Bueno, O. / Prota, A.E. / Bargsten, K. / Saez-Calvo, G. / Jimeno, M.L. / Benkheil, M. / Ribatti, D. / Velazquez, S. / Camarasa, M.J. / Diaz, J.F. / Steinmetz, M.O. ...Authors: Canela, M.D. / Noppen, S. / Bueno, O. / Prota, A.E. / Bargsten, K. / Saez-Calvo, G. / Jimeno, M.L. / Benkheil, M. / Ribatti, D. / Velazquez, S. / Camarasa, M.J. / Diaz, J.F. / Steinmetz, M.O. / Priego, E.M. / Perez-Perez, M.J. / Liekens, S. |
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History | Deposition | May 11, 2016 | Deposition site: RCSB / Processing site: PDBE |
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Revision 1.0 | Jun 8, 2016 | Provider: repository / Type: Initial release |
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Revision 1.1 | Apr 26, 2017 | Group: Database references |
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Revision 1.2 | Sep 6, 2017 | Group: Author supporting evidence / Structure summary / Category: entity / pdbx_audit_support Item: _entity.pdbx_description / _pdbx_audit_support.funding_organization |
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Revision 1.3 | May 8, 2024 | Group: Data collection / Database references / Derived calculations Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_struct_conn_angle / struct_conn Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_comp_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr2_label_atom_id / _pdbx_struct_conn_angle.ptnr2_label_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id |
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