1n2z
From Proteopedia
(New page: 200px<br /><applet load="1n2z" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n2z, resolution 2.0Å" /> '''2.0 Angstrom structur...) |
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| - | [[Image:1n2z.gif|left|200px]]<br /><applet load="1n2z" size=" | + | [[Image:1n2z.gif|left|200px]]<br /><applet load="1n2z" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1n2z, resolution 2.0Å" /> | caption="1n2z, resolution 2.0Å" /> | ||
'''2.0 Angstrom structure of BtuF, the vitamin B12 binding protein of E. coli'''<br /> | '''2.0 Angstrom structure of BtuF, the vitamin B12 binding protein of E. coli'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Bacterial binding protein-dependent ATP binding cassette (ABC) | + | Bacterial binding protein-dependent ATP binding cassette (ABC) transporters facilitate uptake of essential nutrients. The crystal structure of Escherichia coli BtuF, the protein that binds vitamin B12 and delivers it to the periplasmic surface of the ABC transporter BtuCD, reveals a bi-lobed fold resembling that of the ferrichrome binding protein FhuD. B12 is bound in the "base-on" conformation in a deep cleft formed at the interface between the two lobes of BtuF. A stable complex between BtuF and BtuCD (with the stoichiometry BtuC2D2F) is demonstrated to form in vitro and was modeled using the individual crystal structures. Two surface glutamates from BtuF may interact with arginine residues on the periplasmic surface of the BtuCD transporter. These glutamate and arginine residues are conserved among binding proteins and ABC transporters mediating iron and B12 uptake, suggesting that they may have a role in docking and the transmission of conformational changes. |
==About this Structure== | ==About this Structure== | ||
| - | 1N2Z 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 CD, CL, CNC and PG4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1N2Z 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=CD:'>CD</scene>, <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=CNC:'>CNC</scene> and <scene name='pdbligand=PG4:'>PG4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N2Z OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Borths, E | + | [[Category: Borths, E L.]] |
| - | [[Category: Lee, A | + | [[Category: Lee, A T.]] |
| - | [[Category: Locher, K | + | [[Category: Locher, K P.]] |
| - | [[Category: Rees, D | + | [[Category: Rees, D C.]] |
[[Category: CD]] | [[Category: CD]] | ||
[[Category: CL]] | [[Category: CL]] | ||
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[[Category: transport protein]] | [[Category: transport protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:01:42 2008'' |
Revision as of 12:01, 21 February 2008
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2.0 Angstrom structure of BtuF, the vitamin B12 binding protein of E. coli
Overview
Bacterial binding protein-dependent ATP binding cassette (ABC) transporters facilitate uptake of essential nutrients. The crystal structure of Escherichia coli BtuF, the protein that binds vitamin B12 and delivers it to the periplasmic surface of the ABC transporter BtuCD, reveals a bi-lobed fold resembling that of the ferrichrome binding protein FhuD. B12 is bound in the "base-on" conformation in a deep cleft formed at the interface between the two lobes of BtuF. A stable complex between BtuF and BtuCD (with the stoichiometry BtuC2D2F) is demonstrated to form in vitro and was modeled using the individual crystal structures. Two surface glutamates from BtuF may interact with arginine residues on the periplasmic surface of the BtuCD transporter. These glutamate and arginine residues are conserved among binding proteins and ABC transporters mediating iron and B12 uptake, suggesting that they may have a role in docking and the transmission of conformational changes.
About this Structure
1N2Z is a Single protein structure of sequence from Escherichia coli with , , and as ligands. Full crystallographic information is available from OCA.
Reference
The structure of Escherichia coli BtuF and binding to its cognate ATP binding cassette transporter., Borths EL, Locher KP, Lee AT, Rees DC, Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16642-7. Epub 2002 Dec 10. PMID:12475936
Page seeded by OCA on Thu Feb 21 14:01:42 2008
Categories: Escherichia coli | Single protein | Borths, E L. | Lee, A T. | Locher, K P. | Rees, D C. | CD | CL | CNC | PG4 | Transport protein
