2zd7: Difference between revisions

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<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 [https://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 [https://proteopedia.org/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 ([https://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'>[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>
<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 ==
[[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>
[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]]
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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=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>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Rtt109 is a histone acetyltransferase that requires a histone chaperone for the acetylation of histone 3 at lysine 56 (H3K56). Rtt109 forms a complex with the chaperone Vps75 in vivo and is implicated in DNA replication and repair. Here we show that both Rtt109 and Vps75 bind histones with high affinity, but only the complex is efficient for catalysis. The C-terminal acidic domain of Vps75 contributes to activation of Rtt109 and is necessary for in vivo functionality of Vps75, but it is not required for interaction with either Rtt109 or histones. We demonstrate that Vps75 is a structural homolog of yeast Nap1 by solving its crystal structure. Nap1 and Vps75 interact with histones and Rtt109 with comparable affinities. However, only Vps75 stimulates Rtt109 enzymatic activity. Our data highlight the functional specificity of Vps75 in Rtt109 activation.
Histone chaperone specificity in Rtt109 activation.,Park YJ, Sudhoff KB, Andrews AJ, Stargell LA, Luger K Nat Struct Mol Biol. 2008 Sep;15(9):957-64. PMID:19172749<ref>PMID:19172749</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2zd7" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 18824]]
[[Category: Large Structures]]
[[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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