1s62
From Proteopedia
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| - | [[Image:1s62.gif|left|200px]] | + | [[Image:1s62.gif|left|200px]] |
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| - | '''Solution structure of the Escherichia coli TolA C-terminal domain''' | + | {{Structure |
| + | |PDB= 1s62 |SIZE=350|CAPTION= <scene name='initialview01'>1s62</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= TOLA, CIM, EXCC, LKY, B0739 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | }} | ||
| + | |||
| + | '''Solution structure of the Escherichia coli TolA C-terminal domain''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1S62 is a [ | + | 1S62 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=1S62 OCA]. |
==Reference== | ==Reference== | ||
| - | Solution structure of the E.coli TolA C-terminal domain reveals conformational changes upon binding to the phage g3p N-terminal domain., Deprez C, Lloubes R, Gavioli M, Marion D, Guerlesquin F, Blanchard L, J Mol Biol. 2005 Mar 4;346(4):1047-57. Epub 2005 Jan 12. PMID:[http:// | + | Solution structure of the E.coli TolA C-terminal domain reveals conformational changes upon binding to the phage g3p N-terminal domain., Deprez C, Lloubes R, Gavioli M, Marion D, Guerlesquin F, Blanchard L, J Mol Biol. 2005 Mar 4;346(4):1047-57. Epub 2005 Jan 12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15701516 15701516] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: tol g3p interaction]] | [[Category: tol g3p interaction]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:00:57 2008'' |
Revision as of 12:00, 20 March 2008
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| Gene: | TOLA, CIM, EXCC, LKY, B0739 (Escherichia coli) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Solution structure of the Escherichia coli TolA C-terminal domain
Overview
The Tol-Pal system of Escherichia coli is a macromolecular complex located in the cell envelope. It is involved in maintaining the integrity of the outer membrane and is required for the uptake of two different types of macromolecules, which are bacteriotoxins (colicins) and DNA of filamentous bacteriophages. The TolA protein plays a central role in these import mechanisms. Its C-terminal domain (TolAIII) is involved in the translocation step via direct interaction with the N-terminal domain of colicins and the N-terminal domain of the phage minor coat gene 3 protein (g3pN1). Extreme behaviours of TolAIII have been previously observed, since the structure of TolAIII either remained unaffected or adopted disordered conformation upon binding to different pore-forming colicins. Here, we have solved the 3D structure of free TolAIII by heteronuclear NMR spectroscopy and compared it to the crystal structure of TolAIII bound to g3pN1 in order to study the effect of g3pN1 on the tertiary structure of TolAIII. Backbone 1H, 15N and 13C resonances of the g3pN1-bound TolAIII were also assigned and used to superimpose the solution structure of free TolAIII on the crystal structure of the g3pN1-TolAIII fusion protein. This allowed us to track conformational changes of TolAIII upon binding. While the global fold of free TolAIII is mainly identical to that of g3pN1-bound TolAIII, shift of secondary structures does occur. Thus, TolAIII, which interacts also in vivo with Pal and TolB, is able to adapt its conformation upon binding to various partners. Possible models for protein binding mechanisms are discussed to explain this so-far unobserved behaviour of TolAIII.
About this Structure
1S62 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Solution structure of the E.coli TolA C-terminal domain reveals conformational changes upon binding to the phage g3p N-terminal domain., Deprez C, Lloubes R, Gavioli M, Marion D, Guerlesquin F, Blanchard L, J Mol Biol. 2005 Mar 4;346(4):1047-57. Epub 2005 Jan 12. PMID:15701516
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