Entry | Database: PDB / ID: 6cvl |
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Title | Crystal structure of the Escherichia coli ATPgS-bound MetNI methionine ABC transporter in complex with its MetQ binding protein |
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Components | - MetI transmembrane subunit
- MetN nucleotide-binding subunit
- MetQ periplasmic binding protein
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Keywords | MEMBRANE PROTEIN / MetNIQ / Outward-facing conformation / Catalytic intermediate state |
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Function / homology | Function and homology information
L-methionine transmembrane transporter activity / ABC-type D-methionine transporter activity / methionine import across plasma membrane / methionine-importing ABC transporter complex / ABC-type methionine transporter / D-methionine transmembrane transport / Gram-negative-bacterium-type cell wall / ATPase-coupled transmembrane transporter activity / metabolic process / ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing ...L-methionine transmembrane transporter activity / ABC-type D-methionine transporter activity / methionine import across plasma membrane / methionine-importing ABC transporter complex / ABC-type methionine transporter / D-methionine transmembrane transport / Gram-negative-bacterium-type cell wall / ATPase-coupled transmembrane transporter activity / metabolic process / ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing / outer membrane-bounded periplasmic space / ATP hydrolysis activity / ATP binding / membrane / plasma membraneSimilarity search - Function ABC transporter, methionine import, ATP-binding protein MetN, proteobacteria / NIL domain / NIL domain / Methionine import ATP-binding protein metN family profile. / NIL / Methionine import ATP-binding protein MetN, ATP-binding domain / Lipoprotein NlpA family / NlpA lipoprotein / MetI-like fold / MetI-like ...ABC transporter, methionine import, ATP-binding protein MetN, proteobacteria / NIL domain / NIL domain / Methionine import ATP-binding protein metN family profile. / NIL / Methionine import ATP-binding protein MetN, ATP-binding domain / Lipoprotein NlpA family / NlpA lipoprotein / MetI-like fold / MetI-like / ABC transporter type 1, transmembrane domain MetI-like / MetI-like superfamily / Binding-protein-dependent transport system inner membrane component / ABC transporter integral membrane type-1 domain profile. / ACT domain / ACT-like domain / ABC transporter-like, conserved site / ABC transporters family signature. / Periplasmic binding protein-like II / ABC transporter / ABC transporter-like, ATP-binding domain / ATP-binding cassette, ABC transporter-type domain profile. / D-Maltodextrin-Binding Protein; domain 2 / Prokaryotic membrane lipoprotein lipid attachment site profile. / P-loop containing nucleotide triphosphate hydrolases / Alpha-Beta Plaits / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / P-loop containing nucleoside triphosphate hydrolase / Rossmann fold / 2-Layer Sandwich / Orthogonal Bundle / 3-Layer(aba) Sandwich / Mainly Alpha / Alpha BetaSimilarity search - Domain/homology PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER / : / IODIDE ION / D-methionine-binding lipoprotein MetQ / Methionine import ATP-binding protein MetN / D-methionine transport system permease protein MetISimilarity search - Component |
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Biological species | ![](img/tx_bacteria.gif) Escherichia coli (E. coli) |
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Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / SAD / molecular replacement / Resolution: 2.953 Å |
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Authors | Nguyen, P.T. / Kaiser, J.T. / Rees, D.C. |
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Funding support | United States, Viet Nam, 2items Organization | Grant number | Country |
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Howard Hughes Medical Institute (HHMI) | | United States | Vietnam International Education Development | | Viet Nam |
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Citation | Journal: Proc. Natl. Acad. Sci. U.S.A. / Year: 2018 Title: Noncanonical role for the binding protein in substrate uptake by the MetNI methionine ATP Binding Cassette (ABC) transporter. Authors: Nguyen, P.T. / Lai, J.Y. / Lee, A.T. / Kaiser, J.T. / Rees, D.C. |
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History | Deposition | Mar 28, 2018 | Deposition site: RCSB / Processing site: RCSB |
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Revision 1.0 | Nov 14, 2018 | Provider: repository / Type: Initial release |
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Revision 1.1 | Nov 20, 2019 | Group: Advisory / Author supporting evidence / Category: pdbx_audit_support / pdbx_database_PDB_obs_spr / Item: _pdbx_audit_support.funding_organization |
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Revision 1.2 | Apr 27, 2022 | Group: Advisory / Database references / Derived calculations Category: database_2 / pdbx_database_PDB_obs_spr / struct_conn Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _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.ptnr1_symmetry / _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 / _struct_conn.ptnr2_label_seq_id / _struct_conn.ptnr2_symmetry |
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Revision 1.3 | May 22, 2024 | Group: Data collection / Refinement description Category: chem_comp_atom / chem_comp_bond / struct_ncs_dom_lim Item: _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_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 |
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