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3gq2

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Revision as of 19:13, 24 December 2014

Crystal Structure of the Dimer of the p115 Tether Globular Head Domain

Structural highlights

3gq2 is a 2 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	p115, USO1, VDP (Bos taurus)
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[USO1_BOVIN] General vesicular transport factor required for intercisternal transport in the Golgi stack; it is required for transcytotic fusion and/or subsequent binding of the vesicles to the target membrane. May well act as a vesicular anchor by interacting with the target membrane and holding the vesicular and target membranes in proximity.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Molecular tethers have a central role in the organization of the complex membrane architecture of eukaryotic cells. p115 is a ubiquitous, essential tether involved in vesicle transport and the structural organization of the exocytic pathway. We describe two crystal structures of the N-terminal domain of p115 at 2.0 A resolution. The p115 structures show a novel alpha-solenoid architecture constructed of 12 armadillo-like, tether-repeat, alpha-helical tripod motifs. We find that the H1 TR binds the Rab1 GTPase involved in endoplasmic reticulum to Golgi transport. Mutation of the H1 motif results in the dominant negative inhibition of endoplasmic reticulum to Golgi trafficking. We propose that the H1 helical tripod contributes to the assembly of Rab-dependent complexes responsible for the tether and SNARE-dependent fusion of membranes.

Structural and functional analysis of the globular head domain of p115 provides insight into membrane tethering.,An Y, Chen CY, Moyer B, Rotkiewicz P, Elsliger MA, Godzik A, Wilson IA, Balch WE J Mol Biol. 2009 Aug 7;391(1):26-41. Epub 2009 May 4. PMID:19414022^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ An Y, Chen CY, Moyer B, Rotkiewicz P, Elsliger MA, Godzik A, Wilson IA, Balch WE. Structural and functional analysis of the globular head domain of p115 provides insight into membrane tethering. J Mol Biol. 2009 Aug 7;391(1):26-41. Epub 2009 May 4. PMID:19414022 doi:10.1016/j.jmb.2009.04.062

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3gq2"

@@ Line 6: / Line 6: @@
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3gq2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gq2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3gq2 RCSB], [http://www.ebi.ac.uk/pdbsum/3gq2 PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/USO1_BOVIN USO1_BOVIN]] General vesicular transport factor required for intercisternal transport in the Golgi stack; it is required for transcytotic fusion and/or subsequent binding of the vesicles to the target membrane. May well act as a vesicular anchor by interacting with the target membrane and holding the vesicular and target membranes in proximity.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

3gq2

From Proteopedia

Revision as of 19:13, 24 December 2014

Crystal Structure of the Dimer of the p115 Tether Globular Head Domain

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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