1u07: Difference between revisions

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[[Image:1u07.gif|left|200px]]<br /><applet load="1u07" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1u07.gif|left|200px]]<br /><applet load="1u07" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1u07, resolution 1.13Å" />

'''Crystal Structure of the 92-residue C-term. part of TonB with significant structural changes compared to shorter fragments'''<br />

==Overview==

Uptake of siderophores and vitamin B(12) through the outer membrane of, Escherichia coli is effected by an active transport system consisting of, several outer membrane receptors and a protein complex of the inner, membrane. The link between these is TonB, a protein associated with the, cytoplasmic membrane, which forms a large periplasmic domain capable of, interacting with several outer membrane receptors, e.g. FhuA, FecA, and, FepA for siderophores and BtuB for vitamin B(12.) The active transport, across the outer membrane is driven by the chemiosmotic gradient of the, inner membrane and is mediated by the TonB protein. The receptor-binding, domain of TonB appears to be formed by a highly conserved C-terminal amino, acid sequence of approximately 100 residues. Crystal structures of two, C-terminal TonB fragments composed of 85 (TonB-85) and 77 (TonB-77) amino, acid residues, respectively, have been previously determined (Chang, C., Mooser, A., Pluckthun, A., and Wlodawer, A. (2001) J. Biol. Chem. 276, 27535-27540 and Koedding, J., Howard, S. P., Kaufmann, L., Polzer, P., Lustig, A., and Welte, W. (2004) J. Biol. Chem. 279, 9978-9986). In both, cases the TonB fragments form dimers in solution and crystallize as dimers, consisting of monomers tightly engaged with one another by the exchange of, a beta-hairpin and a C-terminal beta-strand. Here we present the crystal, structure of a 92-residue fragment of TonB (TonB-92), which is monomeric, in solution. The structure, determined at 1.13-A resolution, shows a dimer, with considerably reduced intermolecular interaction compared with the, other known TonB structures, in particular lacking the beta-hairpin, exchange.

Uptake of siderophores and vitamin B(12) through the outer membrane of Escherichia coli is effected by an active transport system consisting of several outer membrane receptors and a protein complex of the inner membrane. The link between these is TonB, a protein associated with the cytoplasmic membrane, which forms a large periplasmic domain capable of interacting with several outer membrane receptors, e.g. FhuA, FecA, and FepA for siderophores and BtuB for vitamin B(12.) The active transport across the outer membrane is driven by the chemiosmotic gradient of the inner membrane and is mediated by the TonB protein. The receptor-binding domain of TonB appears to be formed by a highly conserved C-terminal amino acid sequence of approximately 100 residues. Crystal structures of two C-terminal TonB fragments composed of 85 (TonB-85) and 77 (TonB-77) amino acid residues, respectively, have been previously determined (Chang, C., Mooser, A., Pluckthun, A., and Wlodawer, A. (2001) J. Biol. Chem. 276, 27535-27540 and Koedding, J., Howard, S. P., Kaufmann, L., Polzer, P., Lustig, A., and Welte, W. (2004) J. Biol. Chem. 279, 9978-9986). In both cases the TonB fragments form dimers in solution and crystallize as dimers consisting of monomers tightly engaged with one another by the exchange of a beta-hairpin and a C-terminal beta-strand. Here we present the crystal structure of a 92-residue fragment of TonB (TonB-92), which is monomeric in solution. The structure, determined at 1.13-A resolution, shows a dimer with considerably reduced intermolecular interaction compared with the other known TonB structures, in particular lacking the beta-hairpin exchange.

==About this Structure==

1U07 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1U07 OCA].

1U07 is a [http://en.wikipedia.org/wiki/Single_protein 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=1U07 OCA].

==Reference==

Line 14:

[[Category: Single protein]]

[[Category: Diederichs, K.]]

[[Category: Howard, S.P.]]

[[Category: Howard, S P.]]

[[Category: Killig, F.]]

[[Category: Koedding, J.]]

Line 21:

[[Category: beta-hairpin]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:19:15 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1u07.gif|left|200px]]<br /><applet load="1u07" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1u07.gif|left|200px]]<br /><applet load="1u07" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1u07, resolution 1.13&Aring;" />
 '''Crystal Structure of the 92-residue C-term. part of TonB with significant structural changes compared to shorter fragments'''<br />
 ==Overview==
-Uptake of siderophores and vitamin B(12) through the outer membrane of, Escherichia coli is effected by an active transport system consisting of, several outer membrane receptors and a protein complex of the inner, membrane. The link between these is TonB, a protein associated with the, cytoplasmic membrane, which forms a large periplasmic domain capable of, interacting with several outer membrane receptors, e.g. FhuA, FecA, and, FepA for siderophores and BtuB for vitamin B(12.) The active transport, across the outer membrane is driven by the chemiosmotic gradient of the, inner membrane and is mediated by the TonB protein. The receptor-binding, domain of TonB appears to be formed by a highly conserved C-terminal amino, acid sequence of approximately 100 residues. Crystal structures of two, C-terminal TonB fragments composed of 85 (TonB-85) and 77 (TonB-77) amino, acid residues, respectively, have been previously determined (Chang, C., Mooser, A., Pluckthun, A., and Wlodawer, A. (2001) J. Biol. Chem. 276, 27535-27540 and Koedding, J., Howard, S. P., Kaufmann, L., Polzer, P., Lustig, A., and Welte, W. (2004) J. Biol. Chem. 279, 9978-9986). In both, cases the TonB fragments form dimers in solution and crystallize as dimers, consisting of monomers tightly engaged with one another by the exchange of, a beta-hairpin and a C-terminal beta-strand. Here we present the crystal, structure of a 92-residue fragment of TonB (TonB-92), which is monomeric, in solution. The structure, determined at 1.13-A resolution, shows a dimer, with considerably reduced intermolecular interaction compared with the, other known TonB structures, in particular lacking the beta-hairpin, exchange.
+Uptake of siderophores and vitamin B(12) through the outer membrane of Escherichia coli is effected by an active transport system consisting of several outer membrane receptors and a protein complex of the inner membrane. The link between these is TonB, a protein associated with the cytoplasmic membrane, which forms a large periplasmic domain capable of interacting with several outer membrane receptors, e.g. FhuA, FecA, and FepA for siderophores and BtuB for vitamin B(12.) The active transport across the outer membrane is driven by the chemiosmotic gradient of the inner membrane and is mediated by the TonB protein. The receptor-binding domain of TonB appears to be formed by a highly conserved C-terminal amino acid sequence of approximately 100 residues. Crystal structures of two C-terminal TonB fragments composed of 85 (TonB-85) and 77 (TonB-77) amino acid residues, respectively, have been previously determined (Chang, C., Mooser, A., Pluckthun, A., and Wlodawer, A. (2001) J. Biol. Chem. 276, 27535-27540 and Koedding, J., Howard, S. P., Kaufmann, L., Polzer, P., Lustig, A., and Welte, W. (2004) J. Biol. Chem. 279, 9978-9986). In both cases the TonB fragments form dimers in solution and crystallize as dimers consisting of monomers tightly engaged with one another by the exchange of a beta-hairpin and a C-terminal beta-strand. Here we present the crystal structure of a 92-residue fragment of TonB (TonB-92), which is monomeric in solution. The structure, determined at 1.13-A resolution, shows a dimer with considerably reduced intermolecular interaction compared with the other known TonB structures, in particular lacking the beta-hairpin exchange.
 ==About this Structure==
-U07 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1U07 OCA].
+U07 is a [http://en.wikipedia.org/wiki/Single_protein 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=1U07 OCA].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: Single protein]]
 [[Category: Diederichs, K.]]
-[[Category: Howard, S.P.]]
+[[Category: Howard, S P.]]
 [[Category: Killig, F.]]
 [[Category: Koedding, J.]]
@@ Line 21: / Line 21: @@
 [[Category: beta-hairpin]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:44:25 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:19:15 2008''