2gsk
From Proteopedia
(New page: 200px<br /><applet load="2gsk" size="450" color="white" frame="true" align="right" spinBox="true" caption="2gsk, resolution 2.10Å" /> '''Structure of the Btu...) |
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| - | [[Image:2gsk.gif|left|200px]]<br /><applet load="2gsk" size=" | + | [[Image:2gsk.gif|left|200px]]<br /><applet load="2gsk" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2gsk, resolution 2.10Å" /> | caption="2gsk, resolution 2.10Å" /> | ||
'''Structure of the BtuB:TonB Complex'''<br /> | '''Structure of the BtuB:TonB Complex'''<br /> | ||
==Overview== | ==Overview== | ||
| - | In Gram-negative bacteria, the import of essential micronutrients across | + | In Gram-negative bacteria, the import of essential micronutrients across the outer membrane requires a transporter, an electrochemical gradient of protons across the inner membrane, and an inner membrane protein complex (ExbB, ExbD, TonB) that couples the proton-motive force to the outer membrane transporter. The inner membrane protein TonB binds directly to a conserved region, called the Ton-box, of the transporter. We solved the structure of the cobalamin transporter BtuB in complex with the C-terminal domain of TonB. In contrast to its conformations in the absence of TonB, the Ton-box forms a beta strand that is recruited to the existing beta sheet of TonB, which is consistent with a mechanical pulling model of transport. |
==About this Structure== | ==About this Structure== | ||
| - | 2GSK is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with CA, CNC, LDA, OCT and HEX as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 2GSK is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=CNC:'>CNC</scene>, <scene name='pdbligand=LDA:'>LDA</scene>, <scene name='pdbligand=OCT:'>OCT</scene> and <scene name='pdbligand=HEX:'>HEX</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GSK OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Banchs, C | + | [[Category: Banchs, C N.]] |
| - | [[Category: Purdy, M | + | [[Category: Purdy, M P.]] |
| - | [[Category: Shultis, D | + | [[Category: Shultis, D D.]] |
| - | [[Category: Wiener, M | + | [[Category: Wiener, M C.]] |
[[Category: CA]] | [[Category: CA]] | ||
[[Category: CNC]] | [[Category: CNC]] | ||
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[[Category: tonb]] | [[Category: tonb]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:34:52 2008'' |
Revision as of 15:34, 21 February 2008
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Structure of the BtuB:TonB Complex
Overview
In Gram-negative bacteria, the import of essential micronutrients across the outer membrane requires a transporter, an electrochemical gradient of protons across the inner membrane, and an inner membrane protein complex (ExbB, ExbD, TonB) that couples the proton-motive force to the outer membrane transporter. The inner membrane protein TonB binds directly to a conserved region, called the Ton-box, of the transporter. We solved the structure of the cobalamin transporter BtuB in complex with the C-terminal domain of TonB. In contrast to its conformations in the absence of TonB, the Ton-box forms a beta strand that is recruited to the existing beta sheet of TonB, which is consistent with a mechanical pulling model of transport.
About this Structure
2GSK is a Protein complex structure of sequences from Escherichia coli with , , , and as ligands. Full crystallographic information is available from OCA.
Reference
Outer membrane active transport: structure of the BtuB:TonB complex., Shultis DD, Purdy MD, Banchs CN, Wiener MC, Science. 2006 Jun 2;312(5778):1396-9. PMID:16741124
Page seeded by OCA on Thu Feb 21 17:34:52 2008
Categories: Escherichia coli | Protein complex | Banchs, C N. | Purdy, M P. | Shultis, D D. | Wiener, M C. | CA | CNC | HEX | LDA | OCT | Beta-barrel | Membrane protein | Outer-membrane active transport | Tonb
