3MEA

Crystal structure of the SGF29 in complex with H3K4me3

Summary for 3MEA

• Entry DOI: 10.2210/pdb3mea/pdb
• Related: 3ME9 3MET 3MEU 3MEV 3MEW
• Descriptor: SAGA-associated factor 29 homolog, Histone H3 (3 entities in total)
• Functional Keywords: structural genomics consortium, sgc, nucleus, transcription, transcription regulation, chromosomal protein, dna-binding, nucleosome core
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus : Q96ES7
• Total number of polymer chains: 2
• Total formula weight: 21735.43

Authors

Bian, C.,Xu, C.,Tempel, W.,MacKenzie, F.,Bountra, C.,Weigelt, J.,Arrowsmith, C.H.,Edwards, A.M.,Bochkarev, A.,Min, J.,Structural Genomics Consortium (SGC) (deposition date: 2010-03-31, release date: 2010-04-28, Last modification date: 2023-09-06)

Primary citation

Bian, C.,Xu, C.,Ruan, J.,Lee, K.K.,Burke, T.L.,Tempel, W.,Barsyte, D.,Li, J.,Wu, M.,Zhou, B.O.,Fleharty, B.E.,Paulson, A.,Allali-Hassani, A.,Zhou, J.Q.,Mer, G.,Grant, P.A.,Workman, J.L.,Zang, J.,Min, J.
Sgf29 binds histone H3K4me2/3 and is required for SAGA complex recruitment and histone H3 acetylation.
Embo J., 30:2829-2842, 2011

PubMed Abstract: The SAGA (Spt-Ada-Gcn5 acetyltransferase) complex is an important chromatin modifying complex that can both acetylate and deubiquitinate histones. Sgf29 is a novel component of the SAGA complex. Here, we report the crystal structures of the tandem Tudor domains of Saccharomyces cerevisiae and human Sgf29 and their complexes with H3K4me2 and H3K4me3 peptides, respectively, and show that Sgf29 selectively binds H3K4me2/3 marks. Our crystal structures reveal that Sgf29 harbours unique tandem Tudor domains in its C-terminus. The tandem Tudor domains in Sgf29 tightly pack against each other face-to-face with each Tudor domain harbouring a negatively charged pocket accommodating the first residue alanine and methylated K4 residue of histone H3, respectively. The H3A1 and K4me3 binding pockets and the limited binding cleft length between these two binding pockets are the structural determinants in conferring the ability of Sgf29 to selectively recognize H3K4me2/3. Our in vitro and in vivo functional assays show that Sgf29 recognizes methylated H3K4 to recruit the SAGA complex to its targets sites and mediates histone H3 acetylation, underscoring the importance of Sgf29 in gene regulation.

PubMed: 21685874
DOI: 10.1038/emboj.2011.193

Experimental method

X-RAY DIFFRACTION (1.26 Å)