3to9

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of yeast Esa1 E338Q HAT domain bound to coenzyme A with active site lysine acetylated

Structural highlights

3to9 is a 1 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2Å
Ligands:	, , , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ESA1_YEAST Catalytic component of the NuA4 histone acetyltransferase (HAT) complex which is involved in epigenetic transcriptional activation of selected genes principally by acetylation of nucleosomal histones H4, H3, H2B, H2A and H2A variant H2A.Z. Acetylates histone H4 to form H4K5ac, H4K8ac, H4K12ac and H4K16ac, histone H3 to form H3K14ac, histone H2B to form H2BK16ac, histone H2A to form H2AK4ac and H2AK7ac, and histone variant H2A.Z to form H2A.ZK14ac. Acetylation of histone H4 is essential for DNA double-strand break repair through homologous recombination. Involved in cell cycle progression. Recruitment to promoters depends on H3K4me.^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7] ^[8] ^[9]

Publication Abstract from PubMed

The MYST protein lysine acetyltransferases are evolutionarily conserved throughout eukaryotes and acetylate proteins to regulate diverse biological processes including gene regulation, DNA repair, cell-cycle regulation, stem cell homeostasis and development. Here, we demonstrate that MYST protein acetyltransferase activity requires active site lysine autoacetylation. The X-ray crystal structures of yeast Esa1 (yEsa1/KAT5) bound to a bisubstrate H4K16CoA inhibitor and human MOF (hMOF/KAT8/MYST1) reveal that they are autoacetylated at a strictly conserved lysine residue in MYST proteins (yEsa1-K262 and hMOF-K274) in the enzyme active site. The structure of hMOF also shows partial occupancy of K274 in the unacetylated form, revealing that the side chain reorients to a position that engages the catalytic glutamate residue and would block cognate protein substrate binding. Consistent with the structural findings, we present mass spectrometry data and biochemical experiments to demonstrate that this lysine autoacetylation on yEsa1, hMOF and its yeast orthologue, ySas2 (KAT8) occurs in solution and is required for acetylation and protein substrate binding in vitro. We also show that this autoacetylation occurs in vivo and is required for the cellular functions of these MYST proteins. These findings provide an avenue for the autoposttranslational regulation of MYST proteins that is distinct from other acetyltransferases but draws similarities to the phosphoregulation of protein kinases.

MYST protein acetyltransferase activity requires active site lysine autoacetylation.,Yuan H, Rossetto D, Mellert H, Dang W, Srinivasan M, Johnson J, Hodawadekar S, Ding EC, Speicher K, Abshiru N, Perry R, Wu J, Yang C, Zheng YG, Speicher DW, Thibault P, Verreault A, Johnson FB, Berger SL, Sternglanz R, McMahon SB, Cote J, Marmorstein R EMBO J. 2011 Oct 21. doi: 10.1038/emboj.2011.382. PMID:22020126^[10]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Ikeda K, Steger DJ, Eberharter A, Workman JL. Activation domain-specific and general transcription stimulation by native histone acetyltransferase complexes. Mol Cell Biol. 1999 Jan;19(1):855-63. PMID:9858608
↑ Clarke AS, Lowell JE, Jacobson SJ, Pillus L. Esa1p is an essential histone acetyltransferase required for cell cycle progression. Mol Cell Biol. 1999 Apr;19(4):2515-26. PMID:10082517
↑ Vignali M, Steger DJ, Neely KE, Workman JL. Distribution of acetylated histones resulting from Gal4-VP16 recruitment of SAGA and NuA4 complexes. EMBO J. 2000 Jun 1;19(11):2629-40. PMID:10835360 doi:http://dx.doi.org/10.1093/emboj/19.11.2629
↑ Galarneau L, Nourani A, Boudreault AA, Zhang Y, Heliot L, Allard S, Savard J, Lane WS, Stillman DJ, Cote J. Multiple links between the NuA4 histone acetyltransferase complex and epigenetic control of transcription. Mol Cell. 2000 Jun;5(6):927-37. PMID:10911987
↑ Bird AW, Yu DY, Pray-Grant MG, Qiu Q, Harmon KE, Megee PC, Grant PA, Smith MM, Christman MF. Acetylation of histone H4 by Esa1 is required for DNA double-strand break repair. Nature. 2002 Sep 26;419(6905):411-5. PMID:12353039 doi:http://dx.doi.org/10.1038/nature01035
↑ Nourani A, Utley RT, Allard S, Cote J. Recruitment of the NuA4 complex poises the PHO5 promoter for chromatin remodeling and activation. EMBO J. 2004 Jul 7;23(13):2597-607. Epub 2004 Jun 3. PMID:15175650 doi:http://dx.doi.org/10.1038/sj.emboj.7600230
↑ Robert F, Pokholok DK, Hannett NM, Rinaldi NJ, Chandy M, Rolfe A, Workman JL, Gifford DK, Young RA. Global position and recruitment of HATs and HDACs in the yeast genome. Mol Cell. 2004 Oct 22;16(2):199-209. PMID:15494307 doi:http://dx.doi.org/10.1016/j.molcel.2004.09.021
↑ Kobor MS, Venkatasubrahmanyam S, Meneghini MD, Gin JW, Jennings JL, Link AJ, Madhani HD, Rine J. A protein complex containing the conserved Swi2/Snf2-related ATPase Swr1p deposits histone variant H2A.Z into euchromatin. PLoS Biol. 2004 May;2(5):E131. Epub 2004 Mar 23. PMID:15045029 doi:10.1371/journal.pbio.0020131
↑ Tamburini BA, Tyler JK. Localized histone acetylation and deacetylation triggered by the homologous recombination pathway of double-strand DNA repair. Mol Cell Biol. 2005 Jun;25(12):4903-13. PMID:15923609 doi:http://dx.doi.org/25/12/4903
↑ Yuan H, Rossetto D, Mellert H, Dang W, Srinivasan M, Johnson J, Hodawadekar S, Ding EC, Speicher K, Abshiru N, Perry R, Wu J, Yang C, Zheng YG, Speicher DW, Thibault P, Verreault A, Johnson FB, Berger SL, Sternglanz R, McMahon SB, Cote J, Marmorstein R. MYST protein acetyltransferase activity requires active site lysine autoacetylation. EMBO J. 2011 Oct 21. doi: 10.1038/emboj.2011.382. PMID:22020126 doi:10.1038/emboj.2011.382

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3to9"

Categories: Large Structures | Saccharomyces cerevisiae | Ding EC | Marmorstein R | Yuan H

@@ Line 1: / Line 1: @@
 ==Crystal structure of yeast Esa1 E338Q HAT domain bound to coenzyme A with active site lysine acetylated==
-<StructureSection load='3to9' size='340' side='right' caption='[[3to9]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+<StructureSection load='3to9' size='340' side='right'caption='[[3to9]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3to9]] is a 1 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=3TO9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TO9 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3to9]] 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=3TO9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TO9 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAD:CACODYLIC+ACID'>CAD</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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]] 2&#8491;</td></tr>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ALY:N(6)-ACETYLLYSINE'>ALY</scene></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ALY:N(6)-ACETYLLYSINE'>ALY</scene>, <scene name='pdbligand=CAD:CACODYLIC+ACID'>CAD</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3to6|3to6]], [[3to7|3to7]], [[3toa|3toa]], [[3tob|3tob]]</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=3to9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3to9 OCA], [https://pdbe.org/3to9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3to9 RCSB], [https://www.ebi.ac.uk/pdbsum/3to9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3to9 ProSAT]</span></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ESA1, YOR244W, O5257 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histone_acetyltransferase Histone acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.48 2.3.1.48] </span></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=3to9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3to9 OCA], [http://pdbe.org/3to9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3to9 RCSB], [http://www.ebi.ac.uk/pdbsum/3to9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3to9 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/ESA1_YEAST ESA1_YEAST]] Catalytic component of the NuA4 histone acetyltransferase (HAT) complex which is involved in epigenetic transcriptional activation of selected genes principally by acetylation of nucleosomal histones H4, H3, H2B, H2A and H2A variant H2A.Z. Acetylates histone H4 to form H4K5ac, H4K8ac, H4K12ac and H4K16ac, histone H3 to form H3K14ac, histone H2B to form H2BK16ac, histone H2A to form H2AK4ac and H2AK7ac, and histone variant H2A.Z to form H2A.ZK14ac. Acetylation of histone H4 is essential for DNA double-strand break repair through homologous recombination. Involved in cell cycle progression. Recruitment to promoters depends on H3K4me.<ref>PMID:9858608</ref> <ref>PMID:10082517</ref> <ref>PMID:10835360</ref> <ref>PMID:10911987</ref> <ref>PMID:12353039</ref> <ref>PMID:15175650</ref> <ref>PMID:15494307</ref> <ref>PMID:15045029</ref> <ref>PMID:15923609</ref>
+[https://www.uniprot.org/uniprot/ESA1_YEAST ESA1_YEAST] Catalytic component of the NuA4 histone acetyltransferase (HAT) complex which is involved in epigenetic transcriptional activation of selected genes principally by acetylation of nucleosomal histones H4, H3, H2B, H2A and H2A variant H2A.Z. Acetylates histone H4 to form H4K5ac, H4K8ac, H4K12ac and H4K16ac, histone H3 to form H3K14ac, histone H2B to form H2BK16ac, histone H2A to form H2AK4ac and H2AK7ac, and histone variant H2A.Z to form H2A.ZK14ac. Acetylation of histone H4 is essential for DNA double-strand break repair through homologous recombination. Involved in cell cycle progression. Recruitment to promoters depends on H3K4me.<ref>PMID:9858608</ref> <ref>PMID:10082517</ref> <ref>PMID:10835360</ref> <ref>PMID:10911987</ref> <ref>PMID:12353039</ref> <ref>PMID:15175650</ref> <ref>PMID:15494307</ref> <ref>PMID:15045029</ref> <ref>PMID:15923609</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 24: / Line 21: @@
 ==See Also==
-*[[Histone acetyltransferase|Histone acetyltransferase]]
+*[[Histone acetyltransferase 3D structures|Histone acetyltransferase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Atcc 18824]]
+[[Category: Large Structures]]
-[[Category: Histone acetyltransferase]]
+[[Category: Saccharomyces cerevisiae]]
-[[Category: Ding, E C]]
+[[Category: Ding EC]]
-[[Category: Marmorstein, R]]
+[[Category: Marmorstein R]]
-[[Category: Yuan, H]]
+[[Category: Yuan H]]
-[[Category: Myst family]]
-[[Category: Transferase]]

3to9

From Proteopedia

Current revision

Crystal structure of yeast Esa1 E338Q HAT domain bound to coenzyme A with active site lysine acetylated

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

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