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7dd0
From Proteopedia
(Difference between revisions)
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==Crystal structure of the N-terminal domain of TagH from Bacillus subtilis== | ==Crystal structure of the N-terminal domain of TagH from Bacillus subtilis== | ||
| - | <StructureSection load='7dd0' size='340' side='right'caption='[[7dd0]]' scene=''> | + | <StructureSection load='7dd0' size='340' side='right'caption='[[7dd0]], [[Resolution|resolution]] 2.70Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7DD0 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=7DD0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7dd0]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacsu Bacsu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7DD0 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=7DD0 FirstGlance]. <br> |
| - | </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=7dd0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7dd0 OCA], [http://pdbe.org/7dd0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=7dd0 RCSB], [http://www.ebi.ac.uk/pdbsum/7dd0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=7dd0 ProSAT]</span></td></tr> | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tagH, BSU35700 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224308 BACSU])</td></tr> |
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/ ], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=7.5.2.4 7.5.2.4] </span></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=7dd0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7dd0 OCA], [http://pdbe.org/7dd0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=7dd0 RCSB], [http://www.ebi.ac.uk/pdbsum/7dd0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=7dd0 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/TAGH_BACSU TAGH_BACSU]] Part of the ABC transporter complex TagGH involved in teichoic acids export. Responsible for energy coupling to the transport system.[HAMAP-Rule:MF_01715]<ref>PMID:7565096</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Bacterial wall teichoic acids (WTAs) are synthesized intracellularly and exported by a two-component transporter, TagGH, comprising the transmembrane and ATPase subunits TagG and TagH. Here the dimeric structure of the N-terminal domain of TagH (TagH-N) was solved by single-wavelength anomalous diffraction using a selenomethionine-containing crystal, which shows an ATP-binding cassette (ABC) architecture with RecA-like and helical subdomains. Besides significant structural differences from other ABC transporters, a prominent patch of positively charged surface is seen in the center of the TagH-N dimer, suggesting a potential binding site for the glycerol phosphate chain of WTA. The ATPase activity of TagH-N was inhibited by clodronate, a bisphosphonate, in a non-competitive manner, consistent with the proposed WTA-binding site for drug targeting. | ||
| + | |||
| + | Crystal structure of the N-terminal domain of TagH reveals a potential drug targeting site.,Yang CS, Huang WC, Ko TP, Wang YC, Wang AH, Chen Y Biochem Biophys Res Commun. 2021 Jan 15;536:1-6. doi: 10.1016/j.bbrc.2020.12.028., Epub 2020 Dec 22. PMID:33360015<ref>PMID:33360015</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7dd0" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Bacsu]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Chen Y]] | + | [[Category: Chen, Y]] |
| - | [[Category: Ko | + | [[Category: Ko, T P]] |
| - | [[Category: Wang | + | [[Category: Wang, Y C]] |
| - | [[Category: Yang | + | [[Category: Yang, C S]] |
| + | [[Category: Abc transporter]] | ||
| + | [[Category: Atp-binding protein]] | ||
| + | [[Category: Translocase]] | ||
| + | [[Category: Transport protein]] | ||
| + | [[Category: Transprot protein]] | ||
Revision as of 06:05, 20 January 2021
Crystal structure of the N-terminal domain of TagH from Bacillus subtilis
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