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| [[Image:1rh5.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1rh5| PDB=1rh5 | SCENE= }} | | {{STRUCTURE_1rh5| PDB=1rh5 | SCENE= }} |
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| '''The structure of a protein conducting channel'''
| | ===The structure of a protein conducting channel=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_14661030}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 14661030 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_14661030}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Protein translocation]] | | [[Category: Protein translocation]] |
| [[Category: Secy]] | | [[Category: Secy]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:29:32 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 04:48:57 2008'' |
