1c5k: Difference between revisions

<StructureSection load='1c5k' size='340' side='right'caption='[[1c5k]], [[Resolution|resolution]] 2.00&Aring;' scene=''>

<table><tr><td colspan='2'>[[1c5k]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C5K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C5K FirstGlance]. <br>

</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&#8491;</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=1c5k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c5k OCA], [https://pdbe.org/1c5k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c5k RCSB], [https://www.ebi.ac.uk/pdbsum/1c5k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c5k ProSAT]</span></td></tr>

[https://www.uniprot.org/uniprot/TOLB_ECOLI TOLB_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.[HAMAP-Rule:MF_00671]

    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c5/1c5k_consurf.spt"</scriptWhenChecked>

    <text>to colour the structure by Evolutionary Conservation</text>

</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1c5k ConSurf].

BACKGROUND: E colicin proteins have three functional domains, each of which is implicated in one of the stages of killing Escherichia coli cells: receptor binding, translocation and cytotoxicity. The central (R) domain is responsible for receptor-binding activity whereas the N-terminal (T) domain mediates translocation, the process by which the C-terminal cytotoxic domain is transported from the receptor to the site of its cytotoxicity. The translocation of enzymatic E colicins like colicin E9 is dependent upon TolB but the details of the process are not known. RESULTS: We have demonstrated a protein-protein interaction between the T domain of colicin E9 and TolB, an essential component of the tol-dependent translocation system in E. coli, using the yeast two-hybrid system. The crystal structure of TolB, a procaryotic tryptophan-aspartate (WD) repeat protein, reveals an N-terminal alpha + beta domain based on a five-stranded mixed beta sheet and a C-terminal six-bladed beta-propeller domain. CONCLUSIONS: The results suggest that the TolB-box residues of the T domain of colicin E9 interact with the beta-propeller domain of TolB. The protein-protein interactions of other beta-propeller-containing proteins, the yeast yPrp4 protein and G proteins, are mediated by the loops or outer sheets of the propeller blades. The determination of the three-dimensional structure of the T domain-TolB complex and the isolation of mutations in TolB that abolish the interaction with the T domain will reveal fine details of the protein-protein interaction of TolB and the T domain of E colicins.

The structure of TolB, an essential component of the tol-dependent translocation system, and its protein-protein interaction with the translocation domain of colicin E9.,Carr S, Penfold CN, Bamford V, James R, Hemmings AM Structure. 2000 Jan 15;8(1):57-66. PMID:10673426<ref>PMID:10673426</ref>

==See Also==

*[[TolB|TolB]]

== References ==

<references/>

</StructureSection>

[[Category: Large Structures]]

[[Category: Bamford V]]

[[Category: Carr S]]

[[Category: Hemmings AM]]

[[Category: James R]]

[[Category: Penfold CN]]