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dc.contributor.authorHaffke, Matthias
dc.contributor.authorMenzel, Anja
dc.contributor.authorCarius, Yvonne
dc.contributor.authorJahn, Dieter
dc.contributor.authorHeinz, Dirk W
dc.date.accessioned2011-05-09T14:12:58Z
dc.date.available2011-05-09T14:12:58Z
dc.date.issued2010-09
dc.identifier.citationStructures of the nucleotide-binding domain of the human ABCB6 transporter and its complexes with nucleotides. 2010, 66 (Pt 9):979-87 Acta Crystallogr. D Biol. Crystallogr.en
dc.identifier.issn1399-0047
dc.identifier.pmid20823549
dc.identifier.doi10.1107/S0907444910028593
dc.identifier.urihttp://hdl.handle.net/10033/129295
dc.description.abstractThe human ATP-binding cassette (ABC) transporter ABCB6 is involved in haem-precursor transport across the mitochondrial membrane. The crystal structure of its nucleotide-binding domain (NBD) has been determined in the apo form and in complexes with ADP, with ADP and Mg(2+) and with ATP at high resolution. The overall structure is L-shaped and consists of two lobes, consistent with other reported NBD structures. Nucleotide binding is mediated by the highly conserved Tyr599 and the Walker A motif, and induces notable structural changes. Structural comparison with other structurally characterized NBDs and full-length ABC transporters gives the first insight into the possible catalytic mechanism of ABCB6 and the role of the N-terminal helix alpha(1) in full-length ABCB6.
dc.language.isoenen
dc.subject.meshATP-Binding Cassette Transportersen
dc.subject.meshAmino Acid Sequenceen
dc.subject.meshAnimalsen
dc.subject.meshCrystallography, X-Rayen
dc.subject.meshHumansen
dc.subject.meshModels, Molecularen
dc.subject.meshMolecular Sequence Dataen
dc.subject.meshNucleotidesen
dc.subject.meshProtein Interaction Domains and Motifsen
dc.subject.meshProtein Structure, Tertiaryen
dc.subject.meshSequence Alignmenten
dc.subject.meshStructural Homology, Proteinen
dc.titleStructures of the nucleotide-binding domain of the human ABCB6 transporter and its complexes with nucleotides.en
dc.typeArticleen
dc.contributor.departmentHelmholtz Zentrum für Infektionsforschung, Braunschweig, Germany.en
dc.identifier.journalActa crystallographica. Section D, Biological crystallographyen
refterms.dateFOA2018-06-13T01:17:21Z
html.description.abstractThe human ATP-binding cassette (ABC) transporter ABCB6 is involved in haem-precursor transport across the mitochondrial membrane. The crystal structure of its nucleotide-binding domain (NBD) has been determined in the apo form and in complexes with ADP, with ADP and Mg(2+) and with ATP at high resolution. The overall structure is L-shaped and consists of two lobes, consistent with other reported NBD structures. Nucleotide binding is mediated by the highly conserved Tyr599 and the Walker A motif, and induces notable structural changes. Structural comparison with other structurally characterized NBDs and full-length ABC transporters gives the first insight into the possible catalytic mechanism of ABCB6 and the role of the N-terminal helix alpha(1) in full-length ABCB6.


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