1wc9
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Transport protein particle (TRAPP) is a large multiprotein complex, involved in endoplasmic reticulum-to-Golgi and intra-Golgi traffic. TRAPP, specifically and persistently resides on Golgi membranes. Neither the, mechanism of the subcellular localization nor the function of any of the, individual TRAPP components is known. Here, the crystal structure of mouse, Bet3p (bet3), a conserved TRAPP component, reveals a dimeric structure, with hydrophobic channels. The channel entrances are located on a putative, membrane-interacting surface that is distinctively flat, wide and, decorated with positively charged residues. Charge-inversion mutations on, the flat surface of the highly conserved yeast Bet3p led to conditional, lethality, incorrect localization and membrane trafficking defects. A, ... | + | Transport protein particle (TRAPP) is a large multiprotein complex, involved in endoplasmic reticulum-to-Golgi and intra-Golgi traffic. TRAPP, specifically and persistently resides on Golgi membranes. Neither the, mechanism of the subcellular localization nor the function of any of the, individual TRAPP components is known. Here, the crystal structure of mouse, Bet3p (bet3), a conserved TRAPP component, reveals a dimeric structure, with hydrophobic channels. The channel entrances are located on a putative, membrane-interacting surface that is distinctively flat, wide and, decorated with positively charged residues. Charge-inversion mutations on, the flat surface of the highly conserved yeast Bet3p led to conditional, lethality, incorrect localization and membrane trafficking defects. A, channel-blocking mutation led to similar defects. These data delineate a, molecular mechanism of Golgi-specific targeting and anchoring of Bet3p, involving the charged surface and insertion of a Golgi-specific, hydrophobic moiety into the channels. This essential subunit could then, direct other TRAPP components to the Golgi. |
==About this Structure== | ==About this Structure== | ||
| - | 1WC9 is a | + | 1WC9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with MYR and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1WC9 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: vesicle transport]] | [[Category: vesicle transport]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 12:28:24 2007'' |
Revision as of 10:23, 5 November 2007
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THE CRYSTAL STRUCTURE OF TRUNCATED MOUSE BET3P
Overview
Transport protein particle (TRAPP) is a large multiprotein complex, involved in endoplasmic reticulum-to-Golgi and intra-Golgi traffic. TRAPP, specifically and persistently resides on Golgi membranes. Neither the, mechanism of the subcellular localization nor the function of any of the, individual TRAPP components is known. Here, the crystal structure of mouse, Bet3p (bet3), a conserved TRAPP component, reveals a dimeric structure, with hydrophobic channels. The channel entrances are located on a putative, membrane-interacting surface that is distinctively flat, wide and, decorated with positively charged residues. Charge-inversion mutations on, the flat surface of the highly conserved yeast Bet3p led to conditional, lethality, incorrect localization and membrane trafficking defects. A, channel-blocking mutation led to similar defects. These data delineate a, molecular mechanism of Golgi-specific targeting and anchoring of Bet3p, involving the charged surface and insertion of a Golgi-specific, hydrophobic moiety into the channels. This essential subunit could then, direct other TRAPP components to the Golgi.
About this Structure
1WC9 is a Single protein structure of sequence from Mus musculus with MYR and GOL as ligands. Structure known Active Site: AC1. Full crystallographic information is available from OCA.
Reference
Crystal structure of bet3 reveals a novel mechanism for Golgi localization of tethering factor TRAPP., Kim YG, Sohn EJ, Seo J, Lee KJ, Lee HS, Hwang I, Whiteway M, Sacher M, Oh BH, Nat Struct Mol Biol. 2005 Jan;12(1):38-45. Epub 2004 Dec 19. PMID:15608655
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