2rkl

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:23, 21 February 2024) (edit) (undo)
 
(10 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2rkl.jpg|left|200px]]
 
-
{{Structure
+
==Crystal Structure of S.cerevisiae Vta1 C-terminal domain==
-
|PDB= 2rkl |SIZE=350|CAPTION= <scene name='initialview01'>2rkl</scene>, resolution 1.500&Aring;
+
<StructureSection load='2rkl' size='340' side='right'caption='[[2rkl]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
-
|SITE= <scene name='pdbsite=AC1:Mpd+Binding+Site+For+Residue+B+1'>AC1</scene>
+
== Structural highlights ==
-
|LIGAND= <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>
+
<table><tr><td colspan='2'>[[2rkl]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RKL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RKL FirstGlance]. <br>
-
|ACTIVITY=
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
-
|GENE= VTA1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr>
-
|DOMAIN=
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2rkl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rkl OCA], [https://pdbe.org/2rkl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rkl RCSB], [https://www.ebi.ac.uk/pdbsum/2rkl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rkl ProSAT]</span></td></tr>
-
|RELATEDENTRY=[[2rkk|2RKK]]
+
</table>
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2rkl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rkl OCA], [http://www.ebi.ac.uk/pdbsum/2rkl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2rkl RCSB]</span>
+
== Function ==
-
}}
+
[https://www.uniprot.org/uniprot/VTA1_YEAST VTA1_YEAST] Has a role in the formation of the multivesicular body (MVB). Required for the sorting of lipids to form intralumenal vesicles and for fluid-phase transport to the vacuole. Required for sorting the plasma membrane proteins STE2 and STE3 into the MVB. Acts a cofactor of VSP4, promotes the oligomerization of VPS4 and stimulates its ATPase activity by 6- to 8-fold.<ref>PMID:12953057</ref> <ref>PMID:14701806</ref> <ref>PMID:16505166</ref> <ref>PMID:16601096</ref>
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rk/2rkl_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/main_output.php?pdb_ID=2rkl ConSurf].
 +
<div style="clear:both"></div>
-
'''Crystal Structure of S.cerevisiae Vta1 C-terminal domain'''
+
==See Also==
-
 
+
*[[Vacuolar protein sorting-associated protein 3D structures|Vacuolar protein sorting-associated protein 3D structures]]
-
 
+
== References ==
-
==Overview==
+
<references/>
-
The MVB pathway plays essential roles in several eukaryotic cellular processes. Proper function of the MVB pathway requires reversible membrane association of the ESCRTs, a process catalyzed by Vps4 ATPase. Vta1 regulates the Vps4 activity, but its mechanism of action was poorly understood. We report the high-resolution crystal structures of the Did2- and Vps60-binding N-terminal domain and the Vps4-binding C-terminal domain of S. cerevisiae Vta1. The C-terminal domain also mediates Vta1 dimerization and both subunits are required for its function as a Vps4 regulator. Emerging from our analysis is a mechanism of regulation by Vta1 in which the C-terminal domain stabilizes the ATP-dependent double ring assembly of Vps4. In addition, the MIT motif-containing N-terminal domain, projected by a long disordered linker, allows contact between the Vps4 disassembly machinery and the accessory ESCRT-III proteins. This provides an additional level of regulation and coordination for ESCRT-III assembly and disassembly.
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
[[Category: Large Structures]]
-
2RKL is a [[Single protein]] structure of 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=2RKL OCA].
+
-
 
+
-
==Reference==
+
-
Structural basis of Vta1 function in the multivesicular body sorting pathway., Xiao J, Xia H, Zhou J, Azmi IF, Davies BA, Katzmann DJ, Xu Z, Dev Cell. 2008 Jan;14(1):37-49. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18194651 18194651]
+
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
-
[[Category: Single protein]]
+
[[Category: Xia H]]
-
[[Category: Xia, H.]]
+
[[Category: Xiao J]]
-
[[Category: Xiao, J.]]
+
[[Category: Xu Z]]
-
[[Category: Xu, Z.]]
+
[[Category: Zhou J]]
-
[[Category: Zhou, J.]]
+
-
[[Category: cytoplasm]]
+
-
[[Category: dimerization motif]]
+
-
[[Category: endosome]]
+
-
[[Category: lipid transport]]
+
-
[[Category: membrane]]
+
-
[[Category: protein transport]]
+
-
[[Category: transport]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:01:28 2008''
+

Current revision

Crystal Structure of S.cerevisiae Vta1 C-terminal domain

PDB ID 2rkl

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2rkl"
Personal tools