1c5k

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(New page: 200px<br /><applet load="1c5k" size="450" color="white" frame="true" align="right" spinBox="true" caption="1c5k, resolution 2.&Aring;" /> '''THE STRUCTURE OF TOLB,...)
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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 />
'''THE STRUCTURE OF TOLB, AN ESSENTIAL COMPONENT OF THE TOL-DEPENDENT TRANSLOCATION SYSTEM AND ITS INTERACTIONS WITH THE TRANSLOCATION DOMAIN OF COLICIN E9'''<br />
==Overview==
==Overview==
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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.
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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==
==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 YB as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1C5K OCA].
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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].
==Reference==
==Reference==
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[[Category: Bamford, V.]]
[[Category: Bamford, V.]]
[[Category: Carr, S.]]
[[Category: Carr, S.]]
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[[Category: Hemmings, A.M.]]
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[[Category: Hemmings, A M.]]
[[Category: James, R.]]
[[Category: James, R.]]
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[[Category: Penfold, C.N.]]
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[[Category: Penfold, C N.]]
[[Category: YB]]
[[Category: YB]]
[[Category: beta propellor]]
[[Category: beta propellor]]
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[[Category: protein-protein interactions]]
[[Category: protein-protein interactions]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:10:35 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:02:36 2008''

Revision as of 10:02, 21 February 2008

Image:1c5k.gif

1c5k, resolution 2.Å

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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

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 with as ligand. 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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