2e50

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spinqualitylabelsall models 2e50, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure of SET/TAF-1beta/INHAT

Overview

Histone chaperones assemble and disassemble nucleosomes in an, ATP-independent manner and thus regulate the most fundamental step in the, alteration of chromatin structure. The molecular mechanisms underlying, histone chaperone activity remain unclear. To gain insights into these, mechanisms, we solved the crystal structure of the functional domain of, SET/TAF-Ibeta/INHAT at a resolution of 2.3 A. We found that, SET/TAF-Ibeta/INHAT formed a dimer that assumed a "headphone"-like, structure. Each subunit of the SET/TAF-Ibeta/INHAT dimer consisted of an N, terminus, a backbone helix, and an "earmuff" domain. It resembles the, structure of the related protein NAP-1. Comparison of the crystal, structures of SET/TAF-Ibeta/INHAT and NAP-1 revealed that the two proteins, were folded similarly except for an inserted helix. However, their, backbone helices were shaped differently, and the relative dispositions of, the backbone helix and the earmuff domain between the two proteins, differed by approximately 40 degrees . Our biochemical analyses of mutants, revealed that the region of SET/TAF-Ibeta/INHAT that is engaged in histone, chaperone activity is the bottom surface of the earmuff domain, because, this surface bound both core histones and double-stranded DNA. This, overlap or closeness of the activity surface and the binding surfaces, suggests that the specific association among SET/TAF-Ibeta/INHAT, core, histones, and double-stranded DNA is requisite for histone chaperone, activity. These findings provide insights into the possible mechanisms by, which histone chaperones assemble and disassemble nucleosome structures.

About this Structure

2E50 is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

Reference

Relationship between the structure of SET/TAF-Ibeta/INHAT and its histone chaperone activity., Muto S, Senda M, Akai Y, Sato L, Suzuki T, Nagai R, Senda T, Horikoshi M, Proc Natl Acad Sci U S A. 2007 Mar 13;104(11):4285-90. Epub 2007 Mar 6. PMID:17360516

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