4di3: Difference between revisions
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[[ | ==Crystal structure of a 2:1 complex of Treponema pallidum TatP(T) (Tp0957) bound to TatT (Tp0956)== | ||
<StructureSection load='4di3' size='340' side='right' caption='[[4di3]], [[Resolution|resolution]] 3.05Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4di3]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Treponema_pallidum_subsp._pallidum Treponema pallidum subsp. pallidum]. 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> | |||
</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> | |||
<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=161 Treponema pallidum subsp. pallidum]), TP_0956 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=161 Treponema pallidum subsp. pallidum])</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=4di3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4di3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4di3 RCSB], [http://www.ebi.ac.uk/pdbsum/4di3 PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
< | |||
[[Category: Treponema pallidum subsp. pallidum]] | [[Category: Treponema pallidum subsp. pallidum]] | ||
[[Category: Brautigam, C A | [[Category: Brautigam, C A]] | ||
[[Category: Deka, R K | [[Category: Deka, R K]] | ||
[[Category: Norgard, M V | [[Category: Norgard, M V]] | ||
[[Category: Protein-protein complex]] | [[Category: Protein-protein complex]] | ||
[[Category: Tpat]] | [[Category: Tpat]] | ||
[[Category: Transport protein]] | [[Category: Transport protein]] | ||
[[Category: Trap transporter]] | [[Category: Trap transporter]] | ||
Revision as of 12:28, 4 January 2015
Crystal structure of a 2:1 complex of Treponema pallidum TatP(T) (Tp0957) bound to TatT (Tp0956)
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