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| | <StructureSection load='6tqe' size='340' side='right'caption='[[6tqe]], [[Resolution|resolution]] 4.30Å' scene=''> | | <StructureSection load='6tqe' size='340' side='right'caption='[[6tqe]], [[Resolution|resolution]] 4.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6tqe]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TQE OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6TQE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6tqe]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TQE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TQE FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.3Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">yddA, yddA_3, DSI35_15825, ERS007665_02362, ERS007670_02474, ERS023446_03427, ERS027651_03600, ERS027652_02163, ERS027654_01933, ERS027656_03005, ERS027659_02286, ERS027661_01835, ERS027666_01377, ERS124361_03074, EZX46_07135, FDK60_09470, SAMEA2682835_03741, SAMEA2682864_01404, SAMEA2683035_00870 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 "Bacillus tuberculosis" (Zopf 1883) Klein 1884])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6tqe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tqe OCA], [http://pdbe.org/6tqe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6tqe RCSB], [http://www.ebi.ac.uk/pdbsum/6tqe PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6tqe ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6tqe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tqe OCA], [https://pdbe.org/6tqe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6tqe RCSB], [https://www.ebi.ac.uk/pdbsum/6tqe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6tqe ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/BACA_MYCTU BACA_MYCTU] Multi-solute ABC transporter that mediates uptake of unrelated hydrophilic compounds (PubMed:32296172). Can transport vitamin B12 and related corrinoids, and antimicrobial peptides such as bleomycin (PubMed:18996991, PubMed:32296172, PubMed:23407640). Transmembrane domains (TMD) form a pore in the membrane and the ATP-binding domain (NBD) is responsible for energy generation (PubMed:32296172). Contributes to maintenance of chronic infections (PubMed:18996991).<ref>PMID:18996991</ref> <ref>PMID:23407640</ref> <ref>PMID:32296172</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Gati, C]] | + | [[Category: Mycobacterium tuberculosis]] |
| - | [[Category: Guskov, A]] | + | [[Category: Gati C]] |
| - | [[Category: Rempel, S]] | + | [[Category: Guskov A]] |
| - | [[Category: Slotboom, D J]] | + | [[Category: Rempel S]] |
| - | [[Category: Abc transporter]]
| + | [[Category: Slotboom DJ]] |
| - | [[Category: Cobalamin]]
| + | |
| - | [[Category: Exporter fold]]
| + | |
| - | [[Category: Import]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| - | [[Category: Tuberculosis]]
| + | |
| - | [[Category: Vitamin b12]]
| + | |
| Structural highlights
Function
BACA_MYCTU Multi-solute ABC transporter that mediates uptake of unrelated hydrophilic compounds (PubMed:32296172). Can transport vitamin B12 and related corrinoids, and antimicrobial peptides such as bleomycin (PubMed:18996991, PubMed:32296172, PubMed:23407640). Transmembrane domains (TMD) form a pore in the membrane and the ATP-binding domain (NBD) is responsible for energy generation (PubMed:32296172). Contributes to maintenance of chronic infections (PubMed:18996991).[1] [2] [3]
Publication Abstract from PubMed
Mycobacterium tuberculosis (Mtb) is an obligate human pathogen and the causative agent of tuberculosis(1-3). Although Mtb can synthesize vitamin B12 (cobalamin) de novo, uptake of cobalamin has been linked to pathogenesis of tuberculosis(2). Mtb does not encode any characterized cobalamin transporter(4-6); however, the gene rv1819c was found to be essential for uptake of cobalamin(1). This result is difficult to reconcile with the original annotation of Rv1819c as a protein implicated in the transport of antimicrobial peptides such as bleomycin(7). In addition, uptake of cobalamin seems inconsistent with the amino acid sequence, which suggests that Rv1819c has a bacterial ATP-binding cassette (ABC)-exporter fold(1). Here, we present structures of Rv1819c, which reveal that the protein indeed contains the ABC-exporter fold, as well as a large water-filled cavity of about 7,700 A(3), which enables the protein to transport the unrelated hydrophilic compounds bleomycin and cobalamin. On the basis of these structures, we propose that Rv1819c is a multi-solute transporter for hydrophilic molecules, analogous to the multidrug exporters of the ABC transporter family, which pump out structurally diverse hydrophobic compounds from cells(8-11).
A mycobacterial ABC transporter mediates the uptake of hydrophilic compounds.,Rempel S, Gati C, Nijland M, Thangaratnarajah C, Karyolaimos A, de Gier JW, Guskov A, Slotboom DJ Nature. 2020 Apr;580(7803):409-412. doi: 10.1038/s41586-020-2072-8. Epub 2020 Mar, 25. PMID:32296172[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Domenech P, Kobayashi H, LeVier K, Walker GC, Barry CE 3rd. BacA, an ABC transporter involved in maintenance of chronic murine infections with Mycobacterium tuberculosis. J Bacteriol. 2009 Jan;191(2):477-85. PMID:18996991 doi:10.1128/JB.01132-08
- ↑ Gopinath K, Venclovas C, Ioerger TR, Sacchettini JC, McKinney JD, Mizrahi V, Warner DF. A vitamin B₁₂ transporter in Mycobacterium tuberculosis. Open Biol. 2013 Feb 13;3(2):120175. PMID:23407640 doi:10.1098/rsob.120175
- ↑ Rempel S, Gati C, Nijland M, Thangaratnarajah C, Karyolaimos A, de Gier JW, Guskov A, Slotboom DJ. A mycobacterial ABC transporter mediates the uptake of hydrophilic compounds. Nature. 2020 Apr;580(7803):409-412. doi: 10.1038/s41586-020-2072-8. Epub 2020 Mar, 25. PMID:32296172 doi:http://dx.doi.org/10.1038/s41586-020-2072-8
- ↑ Rempel S, Gati C, Nijland M, Thangaratnarajah C, Karyolaimos A, de Gier JW, Guskov A, Slotboom DJ. A mycobacterial ABC transporter mediates the uptake of hydrophilic compounds. Nature. 2020 Apr;580(7803):409-412. doi: 10.1038/s41586-020-2072-8. Epub 2020 Mar, 25. PMID:32296172 doi:http://dx.doi.org/10.1038/s41586-020-2072-8
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