2bjn

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==Overview==
==Overview==
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The TRAPP (transport protein particle) complexes are tethering complexes, that have an important role at the different steps of vesicle transport., Recently, the crystal structures of the TRAPP subunits SEDL and BET3 have, been determined, and we present here the 1.7 Angstroms crystal structure, of human TPC6, a third TRAPP subunit. The protein adopts an, alpha/beta-plait topology and forms a dimer. In spite of low sequence, similarity, the structure of TPC6 strikingly resembles that of BET3. The, similarity is especially prominent at the dimerization interfaces of the, proteins. This suggests heterodimerization of TPC6 and BET3, which is, shown by in vitro and in vivo association studies. Together with TPC5, another TRAPP subunit, TPC6 and BET3 are supposed to constitute a family, of paralogous proteins with closely similar three-dimensional structures, but little sequence similarity among its members.
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The TRAPP (transport protein particle) complexes are tethering complexes that have an important role at the different steps of vesicle transport. Recently, the crystal structures of the TRAPP subunits SEDL and BET3 have been determined, and we present here the 1.7 Angstroms crystal structure of human TPC6, a third TRAPP subunit. The protein adopts an alpha/beta-plait topology and forms a dimer. In spite of low sequence similarity, the structure of TPC6 strikingly resembles that of BET3. The similarity is especially prominent at the dimerization interfaces of the proteins. This suggests heterodimerization of TPC6 and BET3, which is shown by in vitro and in vivo association studies. Together with TPC5, another TRAPP subunit, TPC6 and BET3 are supposed to constitute a family of paralogous proteins with closely similar three-dimensional structures but little sequence similarity among its members.
==About this Structure==
==About this Structure==
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[[Category: Kummel, D.]]
[[Category: Kummel, D.]]
[[Category: Misselwitz, R.]]
[[Category: Misselwitz, R.]]
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[[Category: Mueller, J.J.]]
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[[Category: Mueller, J J.]]
[[Category: Roske, Y.]]
[[Category: Roske, Y.]]
[[Category: GOL]]
[[Category: GOL]]
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[[Category: trapp complex]]
[[Category: trapp complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:24:57 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:38:34 2008''

Revision as of 14:38, 21 February 2008


2bjn, resolution 1.70Å

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X-RAY STRUCTURE OF HUMAN TPC6

Overview

The TRAPP (transport protein particle) complexes are tethering complexes that have an important role at the different steps of vesicle transport. Recently, the crystal structures of the TRAPP subunits SEDL and BET3 have been determined, and we present here the 1.7 Angstroms crystal structure of human TPC6, a third TRAPP subunit. The protein adopts an alpha/beta-plait topology and forms a dimer. In spite of low sequence similarity, the structure of TPC6 strikingly resembles that of BET3. The similarity is especially prominent at the dimerization interfaces of the proteins. This suggests heterodimerization of TPC6 and BET3, which is shown by in vitro and in vivo association studies. Together with TPC5, another TRAPP subunit, TPC6 and BET3 are supposed to constitute a family of paralogous proteins with closely similar three-dimensional structures but little sequence similarity among its members.

About this Structure

2BJN is a Single protein structure of sequence from Homo sapiens with and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

The structure of the TRAPP subunit TPC6 suggests a model for a TRAPP subcomplex., Kummel D, Muller JJ, Roske Y, Misselwitz R, Bussow K, Heinemann U, EMBO Rep. 2005 Aug;6(8):787-93. PMID:16025134

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