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7dd0

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Current revision (10:53, 27 March 2024) (edit) (undo)
 
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<StructureSection load='7dd0' size='340' side='right'caption='[[7dd0]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
<StructureSection load='7dd0' size='340' side='right'caption='[[7dd0]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<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>
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<table><tr><td colspan='2'>[[7dd0]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. 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 [https://proteopedia.org/fgij/fg.htm?mol=7DD0 FirstGlance]. <br>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7dd0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7dd0 OCA], [https://pdbe.org/7dd0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7dd0 RCSB], [https://www.ebi.ac.uk/pdbsum/7dd0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7dd0 ProSAT]</span></td></tr>
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<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>
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</table>
</table>
== Function ==
== Function ==
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[[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>
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[https://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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 7dd0" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bacsu]]
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[[Category: Bacillus subtilis subsp. subtilis str. 168]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Chen, Y]]
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[[Category: Chen Y]]
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[[Category: Ko, T P]]
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[[Category: Ko TP]]
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[[Category: Wang, Y C]]
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[[Category: Wang YC]]
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[[Category: Yang, C S]]
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[[Category: Yang CS]]
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[[Category: Abc transporter]]
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[[Category: Atp-binding protein]]
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[[Category: Translocase]]
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[[Category: Transport protein]]
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[[Category: Transprot protein]]
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Current revision

Crystal structure of the N-terminal domain of TagH from Bacillus subtilis

PDB ID 7dd0

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