2j9u

==2 ANGSTROM X-RAY STRUCTURE OF THE YEAST ESCRT-I VPS28 C-TERMINUS IN COMPLEX WITH THE NZF-N DOMAIN FROM ESCRT-II==

<StructureSection load='2j9u' size='340' side='right' caption='[[2j9u]], [[Resolution|resolution]] 2.00&Aring;' scene=''>

<table><tr><td colspan='2'>[[2j9u]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J9U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2J9U FirstGlance]. <br>

</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>

<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2caz|2caz]], [[2g3k|2g3k]], [[1u5t|1u5t]], [[1w7p|1w7p]], [[2cay|2cay]], [[2j9v|2j9v]], [[2j9w|2j9w]]</td></tr>

<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2j9u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j9u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2j9u RCSB], [http://www.ebi.ac.uk/pdbsum/2j9u PDBsum]</span></td></tr>

<table>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/j9/2j9u_consurf.spt"</scriptWhenChecked>

</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="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

ESCRT (endosomal sorting complex required for transport) complexes orchestrate efficient sorting of ubiquitinated transmembrane receptors to lysosomes via multivesicular bodies (MVBs). Yeast ESCRT-I and ESCRT-II interact directly in vitro; however, this association is not detected in yeast cytosol. To gain understanding of the molecular mechanisms of this link, we have characterised the ESCRT-I/-II supercomplex and determined the crystal structure of its interface. The link is formed by the vacuolar protein sorting (Vps)28 C-terminus (ESCRT-I) binding with nanomolar affinity to the Vps36-NZF-N zinc-finger domain (ESCRT-II). A hydrophobic patch on the Vps28-CT four-helix bundle contacts the hydrophobic knuckles of Vps36-NZF-N. Mutation of the ESCRT-I/-II link results in a cargo-sorting defect in yeast. Interestingly, the two Vps36 NZF domains, NZF-N and NZF-C, despite having the same core fold, use distinct surfaces to bind ESCRT-I or ubiquitinated cargo. We also show that a new component of ESCRT-I, Mvb12 (YGR206W), engages ESCRT-I directly with nanomolar affinity to form a 1:1:1:1 heterotetramer. Mvb12 does not affect the affinity of ESCRT-I for ESCRT-II in vitro. Our data suggest a complex regulatory mechanism for the ESCRT-I/-II link in yeast.

Structural insight into the ESCRT-I/-II link and its role in MVB trafficking.,Gill DJ, Teo H, Sun J, Perisic O, Veprintsev DB, Emr SD, Williams RL EMBO J. 2007 Jan 24;26(2):600-12. Epub 2007 Jan 11. PMID:17215868<ref>PMID:17215868</ref>

== References ==

[[Category: Emr, S D.]]

[[Category: Gill, D J.]]

[[Category: Perisic, O.]]

[[Category: Sun, J.]]

[[Category: Teo, H L.]]

[[Category: Veprintsev, D B.]]

[[Category: Williams, R L.]]

[[Category: Zinc-finger]]