Entry | Database: PDB / ID: 4b86 |
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Title | Crystal structure of the MSL1-MSL2 complex (3.5A) |
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Components | - MALE-SPECIFIC LETHAL 1 HOMOLOG
- MALE-SPECIFIC LETHAL 2 HOMOLOG
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Keywords | GENE REGULATION / DOSAGE COMPENSATION / CHROMATIN |
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Function / homology | Function and homology information
MSL complex / Transferases; Acyltransferases; Aminoacyltransferases / ubiquitin protein ligase activity / HATs acetylate histones / protein ubiquitination / nuclear speck / chromatin remodeling / chromatin binding / positive regulation of DNA-templated transcription / nucleoplasm ...MSL complex / Transferases; Acyltransferases; Aminoacyltransferases / ubiquitin protein ligase activity / HATs acetylate histones / protein ubiquitination / nuclear speck / chromatin remodeling / chromatin binding / positive regulation of DNA-templated transcription / nucleoplasm / nucleus / metal ion bindingSimilarity search - Function Protein male-specific lethal-1 / Protein male-specific lethal-1, dimerisation domain / E3 ubiquitin-protein ligase Msl2, zinc RING finger / E3 ubiquitin-protein ligase Msl2, CXC domain / E3 ubiquitin-protein ligase MSL2 / CXC domain of E3 ubiquitin-protein ligase MSL2 / zinc RING finger of MSL2 / Dimerisation domain of Male-specific-Lethal 1 / PEHE domain / PEHE domain ...Protein male-specific lethal-1 / Protein male-specific lethal-1, dimerisation domain / E3 ubiquitin-protein ligase Msl2, zinc RING finger / E3 ubiquitin-protein ligase Msl2, CXC domain / E3 ubiquitin-protein ligase MSL2 / CXC domain of E3 ubiquitin-protein ligase MSL2 / zinc RING finger of MSL2 / Dimerisation domain of Male-specific-Lethal 1 / PEHE domain / PEHE domain / PEHE / Tesmin/TSO1-like CXC domain / Tesmin/TSO1-like CXC domain / Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #170 / Zinc/RING finger domain, C3HC4 (zinc finger) / Herpes Virus-1 / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / Zinc finger RING-type profile. / Zinc finger, RING-type / Zinc finger, RING/FYVE/PHD-type / Up-down Bundle / 2-Layer Sandwich / Mainly Alpha / Alpha BetaSimilarity search - Domain/homology |
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Biological species | HOMO SAPIENS (human) |
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Method | X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 3.5 Å |
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Authors | Hallacli, E. / Lipp, M. / Georgiev, P. / Spielman, C. / Cusack, S. / Akhtar, A. / Kadlec, J. |
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Citation | Journal: Mol.Cell / Year: 2012 Title: Msl1-Mediated Dimerization of the Dosage Compensation Complex is Essential for Male X-Chromosome Regulation in Drosophila. Authors: Hallacli, E. / Lipp, M. / Georgiev, P. / Spielman, C. / Cusack, S. / Akhtar, A. / Kadlec, J. |
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History | Deposition | Aug 24, 2012 | Deposition site: PDBE / Processing site: PDBE |
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Revision 1.0 | Feb 6, 2013 | Provider: repository / Type: Initial release |
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Revision 1.1 | May 8, 2024 | Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other / Refinement description Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_struct_conn_angle / struct_conn / struct_ncs_dom_lim / struct_site Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_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_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_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_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_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 / _struct_conn.ptnr2_label_seq_id / _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 / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id |
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