1lr0

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(New page: 200px<br /><applet load="1lr0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lr0, resolution 1.914&Aring;" /> '''Pseudomonas aerugin...)
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[[Image:1lr0.gif|left|200px]]<br /><applet load="1lr0" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1lr0, resolution 1.914&Aring;" />
caption="1lr0, resolution 1.914&Aring;" />
'''Pseudomonas aeruginosa TolA Domain III, Seleno-methionine Derivative'''<br />
'''Pseudomonas aeruginosa TolA Domain III, Seleno-methionine Derivative'''<br />
==Overview==
==Overview==
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The crystal structure of the C-terminal domain III of Pseudomonas, aeruginosa TolA has been determined at 1.9 A resolution. The fold is, similar to that of the corresponding domain of Escherichia coli TolA, despite the limited amino acid sequence identity of the two proteins, (20%). A pattern was discerned that conserves the fold of domain III, within the wider TolA family and, moreover, reveals a relationship between, TolA domain III and the C-terminal domain of the TonB transporter, proteins. We propose that the TolA and TonB C-terminal domains have a, common evolutionary origin and are related by means of domain swapping, with interesting mechanistic implications. We have also determined the, overall shape of the didomain, domains II + III, of P.aeruginosa TolA by, solution X-ray scattering. The molecule is monomeric-its elongated, stalk, shape can accommodate the crystal structure of domain III at one end, and, an elongated helical bundle within the portion corresponding to domain II., Based on these data, a model for the periplasmic domains of P.aeruginosa, TolA is presented that may explain the inferred allosteric properties of, members of the TolA family. The mechanisms of TolA-mediated entry of, bateriophages in P.aeruginosa and E.coli are likely to be similar.
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The crystal structure of the C-terminal domain III of Pseudomonas aeruginosa TolA has been determined at 1.9 A resolution. The fold is similar to that of the corresponding domain of Escherichia coli TolA, despite the limited amino acid sequence identity of the two proteins (20%). A pattern was discerned that conserves the fold of domain III within the wider TolA family and, moreover, reveals a relationship between TolA domain III and the C-terminal domain of the TonB transporter proteins. We propose that the TolA and TonB C-terminal domains have a common evolutionary origin and are related by means of domain swapping, with interesting mechanistic implications. We have also determined the overall shape of the didomain, domains II + III, of P.aeruginosa TolA by solution X-ray scattering. The molecule is monomeric-its elongated, stalk shape can accommodate the crystal structure of domain III at one end, and an elongated helical bundle within the portion corresponding to domain II. Based on these data, a model for the periplasmic domains of P.aeruginosa TolA is presented that may explain the inferred allosteric properties of members of the TolA family. The mechanisms of TolA-mediated entry of bateriophages in P.aeruginosa and E.coli are likely to be similar.
==About this Structure==
==About this Structure==
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1LR0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa] with ZN and TRS as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LR0 OCA].
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1LR0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=TRS:'>TRS</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LR0 OCA].
==Reference==
==Reference==
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[[Category: Pseudomonas aeruginosa]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Grossman, J.G.]]
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[[Category: Grossman, J G.]]
[[Category: Luisi, B.]]
[[Category: Luisi, B.]]
[[Category: Mizuguchi, K.]]
[[Category: Mizuguchi, K.]]
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[[Category: Perham, R.N.]]
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[[Category: Perham, R N.]]
[[Category: Sanz, C.]]
[[Category: Sanz, C.]]
[[Category: Shah, A.]]
[[Category: Shah, A.]]
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[[Category: tonb]]
[[Category: tonb]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:47:54 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:47:42 2008''

Revision as of 11:47, 21 February 2008


1lr0, resolution 1.914Å

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Pseudomonas aeruginosa TolA Domain III, Seleno-methionine Derivative

Overview

The crystal structure of the C-terminal domain III of Pseudomonas aeruginosa TolA has been determined at 1.9 A resolution. The fold is similar to that of the corresponding domain of Escherichia coli TolA, despite the limited amino acid sequence identity of the two proteins (20%). A pattern was discerned that conserves the fold of domain III within the wider TolA family and, moreover, reveals a relationship between TolA domain III and the C-terminal domain of the TonB transporter proteins. We propose that the TolA and TonB C-terminal domains have a common evolutionary origin and are related by means of domain swapping, with interesting mechanistic implications. We have also determined the overall shape of the didomain, domains II + III, of P.aeruginosa TolA by solution X-ray scattering. The molecule is monomeric-its elongated, stalk shape can accommodate the crystal structure of domain III at one end, and an elongated helical bundle within the portion corresponding to domain II. Based on these data, a model for the periplasmic domains of P.aeruginosa TolA is presented that may explain the inferred allosteric properties of members of the TolA family. The mechanisms of TolA-mediated entry of bateriophages in P.aeruginosa and E.coli are likely to be similar.

About this Structure

1LR0 is a Single protein structure of sequence from Pseudomonas aeruginosa with and as ligands. Full crystallographic information is available from OCA.

Reference

Structure of the periplasmic domain of Pseudomonas aeruginosa TolA: evidence for an evolutionary relationship with the TonB transporter protein., Witty M, Sanz C, Shah A, Grossmann JG, Mizuguchi K, Perham RN, Luisi B, EMBO J. 2002 Aug 15;21(16):4207-18. PMID:12169623

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