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==Crystal structure of tripartite-type ABC transporter MacB from Acinetobacter baumannii== | ==Crystal structure of tripartite-type ABC transporter MacB from Acinetobacter baumannii== | ||
<StructureSection load='5ws4' size='340' side='right' caption='[[5ws4]], [[Resolution|resolution]] 3.40Å' scene=''> | <StructureSection load='5ws4' size='340' side='right'caption='[[5ws4]], [[Resolution|resolution]] 3.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5ws4]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WS4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WS4 FirstGlance]. <br> | <table><tr><td colspan='2'>[[5ws4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aciba Aciba]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WS4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WS4 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AT4:5-O-[(R)-HYDROXY(THIOPHOSPHONOOXY)PHOSPHORYL]ADENOSINE'>AT4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AT4:5-O-[(R)-HYDROXY(THIOPHOSPHONOOXY)PHOSPHORYL]ADENOSINE'>AT4</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">macB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=470 ACIBA])</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ws4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ws4 OCA], [http://pdbe.org/5ws4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ws4 RCSB], [http://www.ebi.ac.uk/pdbsum/5ws4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ws4 ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ws4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ws4 OCA], [http://pdbe.org/5ws4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ws4 RCSB], [http://www.ebi.ac.uk/pdbsum/5ws4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ws4 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/A0A0D8G707_ACIBA A0A0D8G707_ACIBA]] Part of the tripartite efflux system MacAB-TolC. MacB is a non-canonical ABC transporter that contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP-binding domain (NBD), which is responsible for energy generation. Confers resistance against macrolides.[HAMAP-Rule:MF_01720] | [[http://www.uniprot.org/uniprot/A0A0D8G707_ACIBA A0A0D8G707_ACIBA]] Part of the tripartite efflux system MacAB-TolC. MacB is a non-canonical ABC transporter that contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP-binding domain (NBD), which is responsible for energy generation. Confers resistance against macrolides.[HAMAP-Rule:MF_01720] | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The MacA-MacB-TolC tripartite complex is a transmembrane machine that spans both plasma membrane and outer membrane and actively extrudes substrates, including macrolide antibiotics, virulence factors, peptides and cell envelope precursors. These transport activities are driven by the ATPase MacB, a member of the ATP-binding cassette (ABC) superfamily. Here, we present the crystal structure of MacB at 3.4-A resolution. MacB forms a dimer in which each protomer contains a nucleotide-binding domain and four transmembrane helices that protrude in the periplasm into a binding domain for interaction with the membrane fusion protein MacA. MacB represents an ABC transporter in pathogenic microorganisms with unique structural features. | |||
Crystal structure of tripartite-type ABC transporter MacB from Acinetobacter baumannii.,Okada U, Yamashita E, Neuberger A, Morimoto M, van Veen HW, Murakami S Nat Commun. 2017 Nov 6;8(1):1336. doi: 10.1038/s41467-017-01399-2. PMID:29109439<ref>PMID:29109439</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5ws4" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Aciba]] | |||
[[Category: Large Structures]] | |||
[[Category: Murakami, S]] | [[Category: Murakami, S]] | ||
[[Category: Okada, U]] | [[Category: Okada, U]] | ||
Revision as of 13:02, 1 January 2020
Crystal structure of tripartite-type ABC transporter MacB from Acinetobacter baumanniiCrystal structure of tripartite-type ABC transporter MacB from Acinetobacter baumannii
Structural highlights
Function[A0A0D8G707_ACIBA] Part of the tripartite efflux system MacAB-TolC. MacB is a non-canonical ABC transporter that contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP-binding domain (NBD), which is responsible for energy generation. Confers resistance against macrolides.[HAMAP-Rule:MF_01720] Publication Abstract from PubMedThe MacA-MacB-TolC tripartite complex is a transmembrane machine that spans both plasma membrane and outer membrane and actively extrudes substrates, including macrolide antibiotics, virulence factors, peptides and cell envelope precursors. These transport activities are driven by the ATPase MacB, a member of the ATP-binding cassette (ABC) superfamily. Here, we present the crystal structure of MacB at 3.4-A resolution. MacB forms a dimer in which each protomer contains a nucleotide-binding domain and four transmembrane helices that protrude in the periplasm into a binding domain for interaction with the membrane fusion protein MacA. MacB represents an ABC transporter in pathogenic microorganisms with unique structural features. Crystal structure of tripartite-type ABC transporter MacB from Acinetobacter baumannii.,Okada U, Yamashita E, Neuberger A, Morimoto M, van Veen HW, Murakami S Nat Commun. 2017 Nov 6;8(1):1336. doi: 10.1038/s41467-017-01399-2. PMID:29109439[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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