2nq2
From Proteopedia
(New page: 200px<br /><applet load="2nq2" size="450" color="white" frame="true" align="right" spinBox="true" caption="2nq2, resolution 2.400Å" /> '''An inward-facing co...) |
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| - | [[Image:2nq2.gif|left|200px]]<br /><applet load="2nq2" size=" | + | [[Image:2nq2.gif|left|200px]]<br /><applet load="2nq2" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2nq2, resolution 2.400Å" /> | caption="2nq2, resolution 2.400Å" /> | ||
'''An inward-facing conformation of a putative metal-chelate type ABC transporter.'''<br /> | '''An inward-facing conformation of a putative metal-chelate type ABC transporter.'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of a putative metal-chelate-type adenosine | + | The crystal structure of a putative metal-chelate-type adenosine triphosphate (ATP)-binding cassette (ABC) transporter encoded by genes HI1470 and HI1471 of Haemophilus influenzae has been solved at 2.4 angstrom resolution. The permeation pathway exhibits an inward-facing conformation, in contrast to the outward-facing state previously observed for the homologous vitamin B12 importer BtuCD. Although the structures of both HI1470/1 and BtuCD have been solved in nucleotide-free states, the pairs of ABC subunits in these two structures differ by a translational shift in the plane of the membrane that coincides with a repositioning of the membrane-spanning subunits. The differences observed between these ABC transporters involve relatively modest rearrangements and may serve as structural models for inward- and outward-facing conformations relevant to the alternating access mechanism of substrate translocation. |
==About this Structure== | ==About this Structure== | ||
| - | 2NQ2 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae]. Full crystallographic information is available from [http:// | + | 2NQ2 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NQ2 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Haemophilus influenzae]] | [[Category: Haemophilus influenzae]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Lee, A | + | [[Category: Lee, A T.]] |
| - | [[Category: Locher, K | + | [[Category: Locher, K P.]] |
[[Category: Lum, P.]] | [[Category: Lum, P.]] | ||
| - | [[Category: Pinkett, H | + | [[Category: Pinkett, H P.]] |
| - | [[Category: Rees, D | + | [[Category: Rees, D C.]] |
[[Category: atp-binding protein]] | [[Category: atp-binding protein]] | ||
[[Category: nucleotide binding domain]] | [[Category: nucleotide binding domain]] | ||
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[[Category: transmembrane domain]] | [[Category: transmembrane domain]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:09:39 2008'' |
Revision as of 16:09, 21 February 2008
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An inward-facing conformation of a putative metal-chelate type ABC transporter.
Overview
The crystal structure of a putative metal-chelate-type adenosine triphosphate (ATP)-binding cassette (ABC) transporter encoded by genes HI1470 and HI1471 of Haemophilus influenzae has been solved at 2.4 angstrom resolution. The permeation pathway exhibits an inward-facing conformation, in contrast to the outward-facing state previously observed for the homologous vitamin B12 importer BtuCD. Although the structures of both HI1470/1 and BtuCD have been solved in nucleotide-free states, the pairs of ABC subunits in these two structures differ by a translational shift in the plane of the membrane that coincides with a repositioning of the membrane-spanning subunits. The differences observed between these ABC transporters involve relatively modest rearrangements and may serve as structural models for inward- and outward-facing conformations relevant to the alternating access mechanism of substrate translocation.
About this Structure
2NQ2 is a Protein complex structure of sequences from Haemophilus influenzae. Full crystallographic information is available from OCA.
Reference
An inward-facing conformation of a putative metal-chelate-type ABC transporter., Pinkett HW, Lee AT, Lum P, Locher KP, Rees DC, Science. 2007 Jan 19;315(5810):373-7. Epub 2006 Dec 7. PMID:17158291
Page seeded by OCA on Thu Feb 21 18:09:39 2008
