3qdp: Difference between revisions

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[[Image:3qdp.png|left|200px]]


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==Structural characterization of the interaction of colicin A, colicin N, and TolB with TolAIII translocon==
The line below this paragraph, containing "STRUCTURE_3qdp", creates the "Structure Box" on the page.
<StructureSection load='3qdp' size='340' side='right'caption='[[3qdp]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[3qdp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QDP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QDP FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene>, <scene name='pdbligand=MLZ:N-METHYL-LYSINE'>MLZ</scene></td></tr>
{{STRUCTURE_3qdp|  PDB=3qdp  |  SCENE=  }}
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3qdr|3qdr]]</div></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tolA, cim, excC, lky, b0739, JW0729 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=3qdp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qdp OCA], [https://pdbe.org/3qdp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qdp RCSB], [https://www.ebi.ac.uk/pdbsum/3qdp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qdp ProSAT]</span></td></tr>
</table>
== Function ==
[[https://www.uniprot.org/uniprot/TOLA_ECOLI TOLA_ECOLI]] Involved in the TonB-independent uptake of group A colicins (colicins A, E1, E2, E3, and K). Necessary for the colicins to reach their respective targets after initial binding to the bacteria. Also involved in the translocation of bacteriophage DNA.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The Tol assembly of proteins is an interacting network of proteins located in the Eschericha coli cell envelope that transduces energy and contributes to cell integrity. TolA is central to this network linking the inner and outer membranes by interactions with TolQ, TolR, TolB and Pal. Group A colicins, such as ColA, parasitize the Tol network through interactions with TolA and/or TolB, to facilitate translocation through the cell envelope to reach their cytotoxic site of action. We have determined the first structure of the C-terminal domain of TolA (TolAIII) bound to an N-terminal ColA polypeptide (TA53-107). The interface region of the TA53-107-TolAIII complex consists of polar contacts linking residues R92 to R96 of ColA with residues L375-P380 of TolA which constitutes a beta-strand addition commonly seen in more promiscuous protein-protein contacts. The interface region also includes three cation-pi interactions (Y58-K368, Y90-K379, F94-K396) which have not been observed in any other colicin-Tol protein complex. Mutagenesis of the interface residues of ColA or TolA revealed that the effect on the interaction was cumulative; single mutations of either partner had no effect on ColA activity, whereas mutations of three or more residues significantly reduced ColA activity. Mutagenesis of the aromatic ring component of the cation-pi interacting residues showed Y58 of ColA to be essential for the stability of complex formation. TA53-107 binds on the opposite side of TolAIII to that used by g3p, ColN or TolB, illustrating the flexible nature of TolA as a periplasmic hub protein.


===Structural characterization of the interaction of colicin A, colicin N, and TolB with TolAIII translocon===
Structural evidence that colicin A binds to a novel binding site of TolA in the E.coli periplasm.,Li C, Zhang Y, Vankemmelbeke M, Hecht O, Aleanizy FS, Macdonald C, Moore GR, James R, Penfold CN J Biol Chem. 2012 Apr 9. PMID:22493500<ref>PMID:22493500</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3qdp" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_22493500}}, adds the Publication Abstract to the page
*[[TolA|TolA]]
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== References ==
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<references/>
{{ABSTRACT_PUBMED_22493500}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Ecoli]]
[[3qdp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QDP OCA].
[[Category: Large Structures]]
 
[[Category: Li, C]]
==Reference==
<ref group="xtra">PMID:022493500</ref><references group="xtra"/>
[[Category: Escherichia coli]]
[[Category: Li, C.]]
[[Category: Cola]]
[[Category: Cola]]
[[Category: Colicin]]
[[Category: Colicin]]

Latest revision as of 09:03, 8 June 2022

Structural characterization of the interaction of colicin A, colicin N, and TolB with TolAIII transloconStructural characterization of the interaction of colicin A, colicin N, and TolB with TolAIII translocon

Structural highlights

3qdp is a 1 chain structure with sequence from Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:,
Gene:tolA, cim, excC, lky, b0739, JW0729 (ECOLI)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[TOLA_ECOLI] Involved in the TonB-independent uptake of group A colicins (colicins A, E1, E2, E3, and K). Necessary for the colicins to reach their respective targets after initial binding to the bacteria. Also involved in the translocation of bacteriophage DNA.

Publication Abstract from PubMed

The Tol assembly of proteins is an interacting network of proteins located in the Eschericha coli cell envelope that transduces energy and contributes to cell integrity. TolA is central to this network linking the inner and outer membranes by interactions with TolQ, TolR, TolB and Pal. Group A colicins, such as ColA, parasitize the Tol network through interactions with TolA and/or TolB, to facilitate translocation through the cell envelope to reach their cytotoxic site of action. We have determined the first structure of the C-terminal domain of TolA (TolAIII) bound to an N-terminal ColA polypeptide (TA53-107). The interface region of the TA53-107-TolAIII complex consists of polar contacts linking residues R92 to R96 of ColA with residues L375-P380 of TolA which constitutes a beta-strand addition commonly seen in more promiscuous protein-protein contacts. The interface region also includes three cation-pi interactions (Y58-K368, Y90-K379, F94-K396) which have not been observed in any other colicin-Tol protein complex. Mutagenesis of the interface residues of ColA or TolA revealed that the effect on the interaction was cumulative; single mutations of either partner had no effect on ColA activity, whereas mutations of three or more residues significantly reduced ColA activity. Mutagenesis of the aromatic ring component of the cation-pi interacting residues showed Y58 of ColA to be essential for the stability of complex formation. TA53-107 binds on the opposite side of TolAIII to that used by g3p, ColN or TolB, illustrating the flexible nature of TolA as a periplasmic hub protein.

Structural evidence that colicin A binds to a novel binding site of TolA in the E.coli periplasm.,Li C, Zhang Y, Vankemmelbeke M, Hecht O, Aleanizy FS, Macdonald C, Moore GR, James R, Penfold CN J Biol Chem. 2012 Apr 9. PMID:22493500[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Li C, Zhang Y, Vankemmelbeke M, Hecht O, Aleanizy FS, Macdonald C, Moore GR, James R, Penfold CN. Structural evidence that colicin A binds to a novel binding site of TolA in the E.coli periplasm. J Biol Chem. 2012 Apr 9. PMID:22493500 doi:10.1074/jbc.M112.342246

3qdp, resolution 2.15Å

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