Entry Database : PDB / ID : 6t76 Structure visualization Downloads & linksTitle PII-like protein CutA from Nostoc sp. PCC 7120 in apo form ComponentsPeriplasmic divalent cation tolerance protein Details Keywords SIGNALING PROTEIN / CutA / PII-like / cyanobacteriaFunction / homology Divalent ion tolerance protein, CutA / CutA1 divalent ion tolerance protein / Nitrogen regulatory PII-like, alpha/beta / Nitrogen regulatory protein PII/ATP phosphoribosyltransferase, C-terminal / response to metal ion / Periplasmic divalent cation tolerance protein Function and homology informationBiological species Nostoc sp. (bacteria)Method X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution : 1.9 Å DetailsAuthors Selim, K.A. / Albrecht, R. / Forchhammer, K. / Hartmann, M.D. Funding support Germany, 1items Details Hide detailsOrganization Grant number Country German Research Foundation Fo195/9-2, RTG 1708-2 Germany
CitationJournal : Febs J. / Year : 2021Title : Functional and structural characterization of PII-like protein CutA does not support involvement in heavy metal tolerance and hints at a small-molecule carrying/signaling role.Authors : Selim, K.A. / Tremino, L. / Marco-Marin, C. / Alva, V. / Espinosa, J. / Contreras, A. / Hartmann, M.D. / Forchhammer, K. / Rubio, V. History Deposition Oct 21, 2019 Deposition site : PDBE / Processing site : PDBERevision 1.0 Jul 22, 2020 Provider : repository / Type : Initial releaseRevision 1.1 Feb 24, 2021 Group : Database references / Category : citation / citation_authorItem : _citation.journal_volume / _citation.page_first ... _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.year / _citation_author.identifier_ORCID Revision 2.0 Jun 2, 2021 Group : Advisory / Atomic model ... Advisory / Atomic model / Data collection / Database references / Derived calculations / Other / Polymer sequence / Refinement description / Structure summary Category : atom_site / atom_site_anisotrop ... atom_site / atom_site_anisotrop / entity_poly / pdbx_database_status / pdbx_nonpoly_scheme / pdbx_poly_seq_scheme / pdbx_refine_tls_group / pdbx_unobs_or_zero_occ_atoms / pdbx_unobs_or_zero_occ_residues / pdbx_validate_close_contact / pdbx_validate_rmsd_angle / pdbx_validate_rmsd_bond / pdbx_validate_symm_contact / struct_conf / struct_ref_seq / struct_ref_seq_dif / struct_sheet_range / struct_site / struct_site_gen Item : _atom_site.auth_asym_id / _atom_site_anisotrop.pdbx_auth_asym_id ... _atom_site.auth_asym_id / _atom_site_anisotrop.pdbx_auth_asym_id / _entity_poly.pdbx_strand_id / _pdbx_database_status.pdb_format_compatible / _pdbx_nonpoly_scheme.pdb_strand_id / _pdbx_poly_seq_scheme.pdb_strand_id / _pdbx_refine_tls_group.beg_auth_asym_id / _pdbx_refine_tls_group.beg_auth_seq_id / _pdbx_refine_tls_group.end_auth_asym_id / _pdbx_refine_tls_group.end_auth_seq_id / _pdbx_unobs_or_zero_occ_atoms.auth_asym_id / _pdbx_unobs_or_zero_occ_residues.auth_asym_id / _pdbx_validate_close_contact.auth_asym_id_1 / _pdbx_validate_close_contact.auth_asym_id_2 / _pdbx_validate_rmsd_angle.auth_asym_id_1 / _pdbx_validate_rmsd_angle.auth_asym_id_2 / _pdbx_validate_rmsd_angle.auth_asym_id_3 / _pdbx_validate_rmsd_bond.auth_asym_id_1 / _pdbx_validate_rmsd_bond.auth_asym_id_2 / _pdbx_validate_symm_contact.auth_asym_id_1 / _pdbx_validate_symm_contact.auth_asym_id_2 / _struct_conf.beg_auth_asym_id / _struct_conf.end_auth_asym_id / _struct_ref_seq.pdbx_strand_id / _struct_ref_seq_dif.pdbx_pdb_strand_id / _struct_sheet_range.beg_auth_asym_id / _struct_sheet_range.end_auth_asym_id / _struct_site.details / _struct_site.pdbx_auth_asym_id / _struct_site_gen.auth_asym_id Revision 2.1 Jan 24, 2024 Group : Data collection / Database references / Refinement descriptionCategory : chem_comp_atom / chem_comp_bond ... chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model Item : _database_2.pdbx_DOI / _database_2.pdbx_database_accession
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