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4di3

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==Crystal structure of a 2:1 complex of Treponema pallidum TatP(T) (Tp0957) bound to TatT (Tp0956)==
==Crystal structure of a 2:1 complex of Treponema pallidum TatP(T) (Tp0957) bound to TatT (Tp0956)==
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<StructureSection load='4di3' size='340' side='right' caption='[[4di3]], [[Resolution|resolution]] 3.05&Aring;' scene=''>
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<StructureSection load='4di3' size='340' side='right'caption='[[4di3]], [[Resolution|resolution]] 3.05&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4di3]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Trepa Trepa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DI3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DI3 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4di3]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Treponema_pallidum_subsp._pallidum_str._Nichols Treponema pallidum subsp. pallidum str. Nichols]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DI3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DI3 FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3u64|3u64]], [[3u65|3u65]], [[3di4|3di4]]</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]] 3.05&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TP_0957 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243276 TREPA]), TP_0956 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243276 TREPA])</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=4di3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4di3 OCA], [https://pdbe.org/4di3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4di3 RCSB], [https://www.ebi.ac.uk/pdbsum/4di3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4di3 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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4di3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4di3 OCA], [http://pdbe.org/4di3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4di3 RCSB], [http://www.ebi.ac.uk/pdbsum/4di3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4di3 ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/O83923_TREPA O83923_TREPA]
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Tripartite ATP-independent periplasmic transporters (TRAP-Ts) are bacterial transport systems that have been implicated in the import of small molecules into the cytoplasm. A newly discovered subfamily of TRAP-Ts [tetratricopeptide repeat-protein associated TRAP transporters (TPATs)] has four components. Three are common to both TRAP-Ts and TPATs: the P component, a ligand-binding protein, and a transmembrane symporter apparatus comprising the M and Q components (M and Q are sometimes fused to form a single polypeptide). TPATs are distinguished from TRAP-Ts by the presence of a unique protein called the "T component". In Treponema pallidum, this protein (TatT) is a water-soluble trimer whose protomers are each perforated by a pore. Its respective P component (TatP(T)) interacts with the TatT in vitro and in vivo. In this work, we further characterized this interaction. Co-crystal structures of two complexes between the two proteins confirm that up to three monomers of TatP(T) can bind to the TatT trimer. A putative ligand-binding cleft of TatP(T) aligns with the pore of TatT, strongly suggesting ligand transfer between T and P(T). We used a combination of site-directed mutagenesis and analytical ultracentrifugation to derive thermodynamic parameters for the interactions. These observations confirm that the observed crystallographic interface is recapitulated in solution. These results prompt a hypothesis of the molecular mechanism(s) of hydrophobic ligand transport by the TPATs.
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Structural and Thermodynamic Characterization of the Interaction between Two Periplasmic Treponema pallidum Lipoproteins that are Components of a TPR-Protein-Associated TRAP Transporter (TPAT).,Brautigam CA, Deka RK, Schuck P, Tomchick DR, Norgard MV J Mol Biol. 2012 Apr 11. PMID:22504226<ref>PMID:22504226</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 4di3" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Trepa]]
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[[Category: Large Structures]]
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[[Category: Brautigam, C A]]
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[[Category: Treponema pallidum subsp. pallidum str. Nichols]]
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[[Category: Deka, R K]]
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[[Category: Brautigam CA]]
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[[Category: Norgard, M V]]
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[[Category: Deka RK]]
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[[Category: Protein-protein complex]]
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[[Category: Norgard MV]]
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[[Category: Tpat]]
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[[Category: Transport protein]]
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[[Category: Trap transporter]]
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Current revision

Crystal structure of a 2:1 complex of Treponema pallidum TatP(T) (Tp0957) bound to TatT (Tp0956)

PDB ID 4di3

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