4QQG

Crystal structure of an N-terminal HTATIP fragment

Summary for 4QQG

• Entry DOI: 10.2210/pdb4qqg/pdb
• Descriptor: Histone acetyltransferase KAT5, UNKNOWN ATOM OR ION (2 entities in total)
• Functional Keywords: structural genomics consortium, sgc, transferase
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus : Q92993
• Total number of polymer chains: 7
• Total formula weight: 67291.43

Authors

Liu, Y.,Tempel, W.,Wernimont, A.K.,Dobrovetsky, E.,Bountra, C.,Arrowsmith, C.H.,Edwards, A.M.,Min, J.,Structural Genomics Consortium (SGC) (deposition date: 2014-06-27, release date: 2014-07-09, Last modification date: 2023-09-20)

Primary citation

Zhang, Y.,Lei, M.,Yang, X.,Feng, Y.,Yang, Y.,Loppnau, P.,Li, Y.,Yang, Y.,Min, J.,Liu, Y.
Structural and histone binding studies of the chromo barrel domain of TIP60.
FEBS Lett., 592:1221-1232, 2018

PubMed Abstract: Tat-interactive protein 60 consists of an N-terminal chromo barrel domain (TIP60-CB) and a C-terminal acetyltransferase domain and acetylates histone and nonhistone proteins in diverse cellular processes. While TIP60-CB is thought to recognize histone tails, molecular details of this interaction remain unclear. Here, we attempted a quantitative analysis of the interaction between the human TIP60-CB and histone peptides, but did not observe any detectable binding by either fluorescence polarization or isothermal titration calorimetry assays. We also determined the crystal structure of the TIP60-CB alone. Analysis of the apo-structure reveals a putative peptide-binding site that might be occluded by the basic side chain of a residue in a unique β hairpin between the two N-terminal strands of the β barrel, leading to the inability of TIP60-CB to bind histones.

PubMed: 29494751
DOI: 10.1002/1873-3468.13021

Experimental method

X-RAY DIFFRACTION (2.8 Å)