2zd7: Difference between revisions

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==The structure of VPS75 (Vacuolar protein sorting-associated protein 75)==
==The structure of VPS75 (Vacuolar protein sorting-associated protein 75)==
<StructureSection load='2zd7' size='340' side='right' caption='[[2zd7]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
<StructureSection load='2zd7' size='340' side='right'caption='[[2zd7]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2zd7]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZD7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ZD7 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2zd7]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZD7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZD7 FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VPS75 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</td></tr>
<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=2zd7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zd7 OCA], [http://pdbe.org/2zd7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zd7 RCSB], [http://www.ebi.ac.uk/pdbsum/2zd7 PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2zd7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zd7 OCA], [https://pdbe.org/2zd7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zd7 RCSB], [https://www.ebi.ac.uk/pdbsum/2zd7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zd7 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/VPS75_YEAST VPS75_YEAST]] Histone chaperone which acts as a cofactor stimulating the histone H3 'Lys-56' acetylation by RTT109. May be involved in vacuolar proteins sorting.<ref>PMID:12134085</ref> <ref>PMID:17320445</ref>
[https://www.uniprot.org/uniprot/VPS75_YEAST VPS75_YEAST] Histone chaperone which acts as a cofactor stimulating the histone H3 'Lys-56' acetylation by RTT109. May be involved in vacuolar proteins sorting.<ref>PMID:12134085</ref> <ref>PMID:17320445</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zd/2zd7_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zd/2zd7_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
Line 18: Line 19:
</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=2zd7 ConSurf].
</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=2zd7 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
==See Also==
*[[Vacuolar protein sorting-associated protein 3D structures|Vacuolar protein sorting-associated protein 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 18824]]
[[Category: Large Structures]]
[[Category: Luger, K]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Park, Y J]]
[[Category: Synthetic construct]]
[[Category: Histone chaperone]]
[[Category: Luger K]]
[[Category: Nap1]]
[[Category: Park YJ]]
[[Category: Nucleus]]
[[Category: Phosphoprotein]]
[[Category: Protein transport]]
[[Category: Transport]]
[[Category: Vps75]]

Latest revision as of 16:57, 13 March 2024

The structure of VPS75 (Vacuolar protein sorting-associated protein 75)The structure of VPS75 (Vacuolar protein sorting-associated protein 75)

Structural highlights

2zd7 is a 3 chain structure with sequence from Saccharomyces cerevisiae and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.85Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

VPS75_YEAST Histone chaperone which acts as a cofactor stimulating the histone H3 'Lys-56' acetylation by RTT109. May be involved in vacuolar proteins sorting.[1] [2]

Evolutionary Conservation

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

See Also

References

  1. ↑ Bonangelino CJ, Chavez EM, Bonifacino JS. Genomic screen for vacuolar protein sorting genes in Saccharomyces cerevisiae. Mol Biol Cell. 2002 Jul;13(7):2486-501. PMID:12134085 doi:http://dx.doi.org/10.1091/mbc.02-01-0005
  2. ↑ Tsubota T, Berndsen CE, Erkmann JA, Smith CL, Yang L, Freitas MA, Denu JM, Kaufman PD. Histone H3-K56 acetylation is catalyzed by histone chaperone-dependent complexes. Mol Cell. 2007 Mar 9;25(5):703-12. Epub 2007 Feb 22. PMID:17320445 doi:S1097-2765(07)00086-X

2zd7, resolution 1.85Å

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OCA
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