1c5k

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[[Image:1c5k.gif|left|200px]]<br /><applet load="1c5k" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1c5k.gif|left|200px]]
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caption="1c5k, resolution 2.&Aring;" />
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'''THE STRUCTURE OF TOLB, AN ESSENTIAL COMPONENT OF THE TOL-DEPENDENT TRANSLOCATION SYSTEM AND ITS INTERACTIONS WITH THE TRANSLOCATION DOMAIN OF COLICIN E9'''<br />
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{{Structure
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|PDB= 1c5k |SIZE=350|CAPTION= <scene name='initialview01'>1c5k</scene>, resolution 2.&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=YB:YTTERBIUM (III) ION'>YB</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''THE STRUCTURE OF TOLB, AN ESSENTIAL COMPONENT OF THE TOL-DEPENDENT TRANSLOCATION SYSTEM AND ITS INTERACTIONS WITH THE TRANSLOCATION DOMAIN OF COLICIN E9'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1C5K is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=YB:'>YB</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C5K OCA].
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1C5K is a [[Single protein]] structure of 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=1C5K OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10673426 10673426]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/10673426 10673426]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: beta propellor]]
[[Category: beta propellor]]
[[Category: colicin import]]
[[Category: colicin import]]
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[[Category: protein-protein interactions]]
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[[Category: protein-protein interaction]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:02:36 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:20:04 2008''

Revision as of 08:20, 20 March 2008


PDB ID 1c5k

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, resolution 2.Å
Ligands:
Coordinates: save as pdb, mmCIF, xml



THE STRUCTURE OF TOLB, AN ESSENTIAL COMPONENT OF THE TOL-DEPENDENT TRANSLOCATION SYSTEM AND ITS INTERACTIONS WITH THE TRANSLOCATION DOMAIN OF COLICIN E9


Overview

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.

About this Structure

1C5K is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

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

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