1rh5
From Proteopedia
(New page: 200px<br /><applet load="1rh5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rh5, resolution 3.20Å" /> '''The structure of a p...) |
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| - | [[Image:1rh5.gif|left|200px]]<br /><applet load="1rh5" size=" | + | [[Image:1rh5.gif|left|200px]]<br /><applet load="1rh5" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1rh5, resolution 3.20Å" /> | caption="1rh5, resolution 3.20Å" /> | ||
'''The structure of a protein conducting channel'''<br /> | '''The structure of a protein conducting channel'''<br /> | ||
==Overview== | ==Overview== | ||
| - | A conserved heterotrimeric membrane protein complex, the Sec61 or SecY | + | A conserved heterotrimeric membrane protein complex, the Sec61 or SecY complex, forms a protein-conducting channel, allowing polypeptides to be transferred across or integrated into membranes. We report the crystal structure of the complex from Methanococcus jannaschii at a resolution of 3.2 A. The structure suggests that one copy of the heterotrimer serves as a functional translocation channel. The alpha-subunit has two linked halves, transmembrane segments 1-5 and 6-10, clamped together by the gamma-subunit. A cytoplasmic funnel leading into the channel is plugged by a short helix. Plug displacement can open the channel into an 'hourglass' with a ring of hydrophobic residues at its constriction. This ring may form a seal around the translocating polypeptide, hindering the permeation of other molecules. The structure also suggests mechanisms for signal-sequence recognition and for the lateral exit of transmembrane segments of nascent membrane proteins into lipid, and indicates binding sites for partners that provide the driving force for translocation. |
==About this Structure== | ==About this Structure== | ||
| - | 1RH5 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http:// | + | 1RH5 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RH5 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Methanocaldococcus jannaschii]] | [[Category: Methanocaldococcus jannaschii]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Berg, B | + | [[Category: Berg, B van den.]] |
[[Category: Collinson, I.]] | [[Category: Collinson, I.]] | ||
| - | [[Category: Harrison, S | + | [[Category: Harrison, S C.]] |
[[Category: Hartmann, E.]] | [[Category: Hartmann, E.]] | ||
| - | [[Category: Jr., W | + | [[Category: Jr., W M.Clemons.]] |
[[Category: Modis, Y.]] | [[Category: Modis, Y.]] | ||
| - | [[Category: Rapoport, T | + | [[Category: Rapoport, T A.]] |
[[Category: membrane protein]] | [[Category: membrane protein]] | ||
[[Category: protein channels]] | [[Category: protein channels]] | ||
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[[Category: secy]] | [[Category: secy]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:50:50 2008'' |
Revision as of 12:50, 21 February 2008
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The structure of a protein conducting channel
Overview
A conserved heterotrimeric membrane protein complex, the Sec61 or SecY complex, forms a protein-conducting channel, allowing polypeptides to be transferred across or integrated into membranes. We report the crystal structure of the complex from Methanococcus jannaschii at a resolution of 3.2 A. The structure suggests that one copy of the heterotrimer serves as a functional translocation channel. The alpha-subunit has two linked halves, transmembrane segments 1-5 and 6-10, clamped together by the gamma-subunit. A cytoplasmic funnel leading into the channel is plugged by a short helix. Plug displacement can open the channel into an 'hourglass' with a ring of hydrophobic residues at its constriction. This ring may form a seal around the translocating polypeptide, hindering the permeation of other molecules. The structure also suggests mechanisms for signal-sequence recognition and for the lateral exit of transmembrane segments of nascent membrane proteins into lipid, and indicates binding sites for partners that provide the driving force for translocation.
About this Structure
1RH5 is a Protein complex structure of sequences from Methanocaldococcus jannaschii. Full crystallographic information is available from OCA.
Reference
X-ray structure of a protein-conducting channel., Van den Berg B, Clemons WM Jr, Collinson I, Modis Y, Hartmann E, Harrison SC, Rapoport TA, Nature. 2004 Jan 1;427(6969):36-44. Epub 2003 Dec 3. PMID:14661030
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