2j3t: Difference between revisions
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[[Image: | ==THE CRYSTAL STRUCTURE OF THE BET3-TRS33-BET5-TRS23 COMPLEX.== | ||
<StructureSection load='2j3t' size='340' side='right' caption='[[2j3t]], [[Resolution|resolution]] 2.40Å' scene=''> | |||
== Structural highlights == | |||
[[2j3t]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J3T OCA]. <br> | |||
<b>Related:</b> [[1vpg|1vpg]], [[1wc8|1wc8]], [[1wc9|1wc9]], [[2j3r|2j3r]], [[2j3w|2j3w]], [[2c0j|2c0j]]<br> | |||
<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/j3/2j3t_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | |||
<div style="clear:both"></div> | |||
== Publication Abstract from PubMed == | |||
Transport protein particle (TRAPP) I is a multisubunit vesicle tethering factor composed of seven subunits involved in ER-to-Golgi trafficking. The functional mechanism of the complex and how the subunits interact to form a functional unit are unknown. Here, we have used a multidisciplinary approach that includes X-ray crystallography, electron microscopy, biochemistry, and yeast genetics to elucidate the architecture of TRAPP I. The complex is organized through lateral juxtaposition of the subunits into a flat and elongated particle. We have also localized the site of guanine nucleotide exchange activity to a highly conserved surface encompassing several subunits. We propose that TRAPP I attaches to Golgi membranes with its large flat surface containing many highly conserved residues and forms a platform for protein-protein interactions. This study provides the most comprehensive view of a multisubunit vesicle tethering complex to date, based on which a model for the function of this complex, involving Rab1-GTP and long, coiled-coil tethers, is presented. | |||
The architecture of the multisubunit TRAPP I complex suggests a model for vesicle tethering.,Kim YG, Raunser S, Munger C, Wagner J, Song YL, Cygler M, Walz T, Oh BH, Sacher M Cell. 2006 Nov 17;127(4):817-30. PMID:17110339<ref>PMID:17110339</ref> | |||
The | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
< | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
Revision as of 08:27, 30 April 2014
THE CRYSTAL STRUCTURE OF THE BET3-TRS33-BET5-TRS23 COMPLEX.
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