2cfh

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(New page: 200px<br /> <applet load="2cfh" size="450" color="white" frame="true" align="right" spinBox="true" caption="2cfh, resolution 2.30&Aring;" /> '''STRUCTURE OF THE BE...)
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[[Image:2cfh.gif|left|200px]]<br /><applet load="2cfh" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="2cfh" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="2cfh, resolution 2.30&Aring;" />
caption="2cfh, resolution 2.30&Aring;" />
'''STRUCTURE OF THE BET3-TPC6B CORE OF TRAPP'''<br />
'''STRUCTURE OF THE BET3-TPC6B CORE OF TRAPP'''<br />
==Overview==
==Overview==
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The transport protein particle (TRAPP) complexes are involved in the, tethering process at different trafficking steps of vesicle transport. We, here present the crystal structure of a human Bet3-Tpc6B heterodimer, which represents a core sub-complex in the assembly of TRAPP. We describe, a conserved patch of Tpc6 with uncharged pockets, forming a putative, interaction interface for an anchoring moiety at the Golgi. The structural, and functional comparison of the two paralogs Tpc6A and Tpc6B, only found, in some organisms, indicates redundancy and added complexity of TRAPP, architecture and function. Both iso-complexes, Bet3-Tpc6A and Bet3-Tpc6B, are able to recruit Mum2, a further TRAPP subunit, and we identify the, alpha1-alpha2 loop regions as a binding site for Mum2. Our study reveals, similar stability of the iso-complexes and similar expression patterns of, the tpc6 variants in different mouse organs. These findings raise the, possibility that the Tpc6 paralogs might contribute to the formation of, two distinct TRAPP complexes that differ in function.
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The transport protein particle (TRAPP) complexes are involved in the tethering process at different trafficking steps of vesicle transport. We here present the crystal structure of a human Bet3-Tpc6B heterodimer, which represents a core sub-complex in the assembly of TRAPP. We describe a conserved patch of Tpc6 with uncharged pockets, forming a putative interaction interface for an anchoring moiety at the Golgi. The structural and functional comparison of the two paralogs Tpc6A and Tpc6B, only found in some organisms, indicates redundancy and added complexity of TRAPP architecture and function. Both iso-complexes, Bet3-Tpc6A and Bet3-Tpc6B, are able to recruit Mum2, a further TRAPP subunit, and we identify the alpha1-alpha2 loop regions as a binding site for Mum2. Our study reveals similar stability of the iso-complexes and similar expression patterns of the tpc6 variants in different mouse organs. These findings raise the possibility that the Tpc6 paralogs might contribute to the formation of two distinct TRAPP complexes that differ in function.
==About this Structure==
==About this Structure==
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2CFH is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2CFH OCA].
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2CFH is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CFH OCA].
==Reference==
==Reference==
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[[Category: Henke, N.]]
[[Category: Henke, N.]]
[[Category: Kummel, D.]]
[[Category: Kummel, D.]]
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[[Category: Muller, J.J.]]
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[[Category: Muller, J J.]]
[[Category: Roske, Y.]]
[[Category: Roske, Y.]]
[[Category: bet3]]
[[Category: bet3]]
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[[Category: vesicle tethering]]
[[Category: vesicle tethering]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 21:14:40 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:48:08 2008''

Revision as of 14:48, 21 February 2008


2cfh, resolution 2.30Å

Drag the structure with the mouse to rotate

STRUCTURE OF THE BET3-TPC6B CORE OF TRAPP

Overview

The transport protein particle (TRAPP) complexes are involved in the tethering process at different trafficking steps of vesicle transport. We here present the crystal structure of a human Bet3-Tpc6B heterodimer, which represents a core sub-complex in the assembly of TRAPP. We describe a conserved patch of Tpc6 with uncharged pockets, forming a putative interaction interface for an anchoring moiety at the Golgi. The structural and functional comparison of the two paralogs Tpc6A and Tpc6B, only found in some organisms, indicates redundancy and added complexity of TRAPP architecture and function. Both iso-complexes, Bet3-Tpc6A and Bet3-Tpc6B, are able to recruit Mum2, a further TRAPP subunit, and we identify the alpha1-alpha2 loop regions as a binding site for Mum2. Our study reveals similar stability of the iso-complexes and similar expression patterns of the tpc6 variants in different mouse organs. These findings raise the possibility that the Tpc6 paralogs might contribute to the formation of two distinct TRAPP complexes that differ in function.

About this Structure

2CFH is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structure of the Bet3-Tpc6B core of TRAPP: two Tpc6 paralogs form trimeric complexes with Bet3 and Mum2., Kummel D, Muller JJ, Roske Y, Henke N, Heinemann U, J Mol Biol. 2006 Aug 4;361(1):22-32. Epub 2006 Jun 21. PMID:16828797

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