We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

5j9q

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

Crystal structure of the NuA4 core complex

Structural highlights

5j9q is a 15 chain structure with sequence from Saccharomyces cerevisiae and Saccharomyces cerevisiae S288C. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3.25Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

EAF6_YEAST Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is also involved in DNA repair. Component of the NuA3 histone acetyltransferase complex, that acetylates Lys-14 of histone H3. Recruitment of NuA3 to nucleosomes requires methylated histone H3. In conjunction with the FACT complex, NuA3 may be involved in transcriptional regulation.^[1]

Publication Abstract from PubMed

NuA4 catalyzes the acetylation of nucleosomes at histone H4, which is a well-established epigenetic event, controlling many genomic processes in Saccharomyces cerevisiae. Here we report the crystal structures of the NuA4 core complex and a cryoelectron microscopy structure with the nucleosome. The structures show that the histone-binding pocket of the enzyme is rearranged, suggesting its activation. The enzyme binds the histone tail mainly through the target lysine residue, with a preference for a small residue at the -1 position. The complex engages the nucleosome at the dish face and orients its catalytic pocket close to the H4 tail to achieve selective acetylation. The combined data reveal a space-sequence double recognition mechanism of the histone tails by a modifying enzyme in the context of the nucleosome.

The NuA4 Core Complex Acetylates Nucleosomal Histone H4 through a Double Recognition Mechanism.,Xu P, Li C, Chen Z, Jiang S, Fan S, Wang J, Dai J, Zhu P, Chen Z Mol Cell. 2016 Sep 15;63(6):965-75. doi: 10.1016/j.molcel.2016.07.024. Epub 2016 , Sep 1. PMID:27594449^[2]

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

References

↑ Taverna SD, Ilin S, Rogers RS, Tanny JC, Lavender H, Li H, Baker L, Boyle J, Blair LP, Chait BT, Patel DJ, Aitchison JD, Tackett AJ, Allis CD. Yng1 PHD finger binding to H3 trimethylated at K4 promotes NuA3 HAT activity at K14 of H3 and transcription at a subset of targeted ORFs. Mol Cell. 2006 Dec 8;24(5):785-96. PMID:17157260 doi:http://dx.doi.org/10.1016/j.molcel.2006.10.026
↑ Xu P, Li C, Chen Z, Jiang S, Fan S, Wang J, Dai J, Zhu P, Chen Z. The NuA4 Core Complex Acetylates Nucleosomal Histone H4 through a Double Recognition Mechanism. Mol Cell. 2016 Sep 15;63(6):965-75. doi: 10.1016/j.molcel.2016.07.024. Epub 2016 , Sep 1. PMID:27594449 doi:http://dx.doi.org/10.1016/j.molcel.2016.07.024

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/5j9q"

Categories: Large Structures | Saccharomyces cerevisiae | Saccharomyces cerevisiae S288C | Chen ZC | Xu P

@@ Line 9: / Line 9: @@
 </table>
 == Function ==
-[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>
+[https://www.uniprot.org/uniprot/EAF6_YEAST EAF6_YEAST] Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is also involved in DNA repair. Component of the NuA3 histone acetyltransferase complex, that acetylates Lys-14 of histone H3. Recruitment of NuA3 to nucleosomes requires methylated histone H3. In conjunction with the FACT complex, NuA3 may be involved in transcriptional regulation.<ref>PMID:17157260</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

5j9q

From Proteopedia

Current revision

Crystal structure of the NuA4 core complex

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox