1rhz: Difference between revisions

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[[Image:1rhz.gif|left|200px]]<br /><applet load="1rhz" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1rhz.gif|left|200px]]<br /><applet load="1rhz" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1rhz, resolution 3.50Å" />

'''The structure of a protein conducting channel'''<br />

==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.

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==

1RHZ 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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1RHZ OCA].

1RHZ 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=1RHZ OCA].

==Reference==

Line 13:

[[Category: Methanocaldococcus jannaschii]]

[[Category: Protein complex]]

[[Category: Berg, B.van.den.]]

[[Category: Berg, B van den.]]

[[Category: Collinson, I.]]

[[Category: Harrison, S.C.]]

[[Category: Harrison, S C.]]

[[Category: Hartmann, E.]]

[[Category: Jr., W.M.Clemons.]]

[[Category: Jr., W M.Clemons.]]

[[Category: Modis, Y.]]

[[Category: Rapoport, T.A.]]

[[Category: Rapoport, T A.]]

[[Category: membrane protein]]

[[Category: protein channels]]

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[[Category: secy]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Wed Nov~~ 21 01:36:~~39 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:51:05 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1rhz.gif|left|200px]]<br /><applet load="1rhz" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1rhz.gif|left|200px]]<br /><applet load="1rhz" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1rhz, resolution 3.50&Aring;" />
 '''The structure of a protein conducting channel'''<br />
 ==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.
+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==
-RHZ 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RHZ OCA].
+RHZ 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=1RHZ OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Methanocaldococcus jannaschii]]
 [[Category: Protein complex]]
-[[Category: Berg, B.van.den.]]
+[[Category: Berg, B van den.]]
 [[Category: Collinson, I.]]
-[[Category: Harrison, S.C.]]
+[[Category: Harrison, S C.]]
 [[Category: Hartmann, E.]]
-[[Category: Jr., W.M.Clemons.]]
+[[Category: Jr., W M.Clemons.]]
 [[Category: Modis, Y.]]
-[[Category: Rapoport, T.A.]]
+[[Category: Rapoport, T A.]]
 [[Category: membrane protein]]
 [[Category: protein channels]]
@@ Line 25: / Line 25: @@
 [[Category: secy]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:36:39 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:51:05 2008''