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2rko

From Proteopedia

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{{Seed}}
 
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[[Image:2rko.png|left|200px]]
 
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<!--
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==Crystal Structure of the Vps4p-dimer==
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The line below this paragraph, containing "STRUCTURE_2rko", creates the "Structure Box" on the page.
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<StructureSection load='2rko' size='340' side='right'caption='[[2rko]], [[Resolution|resolution]] 3.35&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2rko]] is a 1 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=2RKO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RKO FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.35&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2rko FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rko OCA], [https://pdbe.org/2rko PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rko RCSB], [https://www.ebi.ac.uk/pdbsum/2rko PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rko ProSAT]</span></td></tr>
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{{STRUCTURE_2rko| PDB=2rko | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/VPS4_YEAST VPS4_YEAST] Involved in the transport of biosynthetic membrane proteins from the prevacuolar/endosomal compartment to the vacuole. Required for multivesicular body (MVB) protein sorting. Catalyzes the ATP-dependent dissociation of class E VPS proteins from endosomal membranes, such as the disassembly of the ESCRT-III complex.<ref>PMID:11329380</ref> <ref>PMID:9155008</ref> <ref>PMID:9606181</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rk/2rko_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2rko ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The vacuolar protein sorting (Vps) pathway, in which Vps4 class I AAA-ATPases play a central role, regulates growth factor receptors, immune response, and developmental signaling, and participates in tumor suppression, apoptosis, and retrovirus budding. We present the first atomic structure of the nucleotide-free yeast His(6)DeltaNVps4p dimer and its AMPPNP (5'-adenylyl-beta,gamma-imidodiphosphate)-bound tetradecamer, derived from a cryo electron microscopy map. Vps4p dimers form two distinct heptameric rings and accommodate AAA cassettes in a head-to-head--not in a head-to-tail-fashion as in class II AAA-ATPases. Our model suggests a mechanism for disassembling ESCRT (endosomal sorting complex required for transport) complexes by movements of substrate-binding domains located at the periphery of the tetradecamer during ATP hydrolysis in one ring, followed by translocation through the central pore and ATP hydrolysis in the second ring.
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===Crystal Structure of the Vps4p-dimer===
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Vacuolar protein sorting: two different functional states of the AAA-ATPase Vps4p.,Hartmann C, Chami M, Zachariae U, de Groot BL, Engel A, Grutter MG J Mol Biol. 2008 Mar 21;377(2):352-63. Epub 2008 Jan 15. PMID:18272179<ref>PMID:18272179</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2rko" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_18272179}}, adds the Publication Abstract to the page
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*[[Vacuolar protein sorting-associated protein 3D structures|Vacuolar protein sorting-associated protein 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 18272179 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_18272179}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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2RKO is a 1 chain 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=2RKO OCA].
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==Reference==
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<ref group="xtra">PMID:18272179</ref><references group="xtra"/>
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Gruetter, M G.]]
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[[Category: Gruetter MG]]
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[[Category: Hartmann, C.]]
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[[Category: Hartmann C]]
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[[Category: Aaa-atpase domain]]
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[[Category: Atp-binding]]
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[[Category: Endosome]]
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[[Category: Membrane]]
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[[Category: Nucleotide-binding]]
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[[Category: Phosphorylation]]
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[[Category: Protein transport]]
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[[Category: Transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 07:57:27 2009''
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Current revision

Crystal Structure of the Vps4p-dimer

PDB ID 2rko

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