5AGC

Crystallographic forms of the Vps75 tetramer

Summary for 5AGC

• Entry DOI: 10.2210/pdb5agc/pdb
• Descriptor: VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 75 (1 entity in total)
• Functional Keywords: transport protein, vps75, vacuolar protein sorting 75, histone chaperone, nap1, chromatin
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
• Cellular location: Nucleus : P53853
• Total number of polymer chains: 4
• Total formula weight: 122624.34

Authors

Hammond, C.M.,Sundaramoorthy, R.,Owen-Hughes, T. (deposition date: 2015-01-29, release date: 2016-03-02, Last modification date: 2024-01-10)

Primary citation

Hammond, C.M.,Sundaramoorthy, R.,Larance, M.,Lamond, A.,Stevens, M.A.,El-Mkami, H.,Norman, D.G.,Owen-Hughes, T.
The Histone Chaperone Vps75 Forms Multiple Oligomeric Assemblies Capable of Mediating Exchange between Histone H3-H4 Tetramers and Asf1-H3-H4 Complexes.
Nucleic Acids Res., 44:6157-, 2016

PubMed Abstract: Vps75 is a histone chaperone that has been historically characterized as homodimer by X-ray crystallography. In this study, we present a crystal structure containing two related tetrameric forms of Vps75 within the crystal lattice. We show Vps75 associates with histones in multiple oligomers. In the presence of equimolar H3-H4 and Vps75, the major species is a reconfigured Vps75 tetramer bound to a histone H3-H4 tetramer. However, in the presence of excess histones, a Vps75 dimer bound to a histone H3-H4 tetramer predominates. We show the Vps75-H3-H4 interaction is compatible with the histone chaperone Asf1 and deduce a structural model of the Vps75-Asf1-H3-H4 (VAH) co-chaperone complex using the Pulsed Electron-electron Double Resonance (PELDOR) technique and cross-linking MS/MS distance restraints. The model provides a molecular basis for the involvement of both Vps75 and Asf1 in Rtt109 catalysed histone H3 K9 acetylation. In the absence of Asf1 this model can be used to generate a complex consisting of a reconfigured Vps75 tetramer bound to a H3-H4 tetramer. This provides a structural explanation for many of the complexes detected biochemically and illustrates the ability of Vps75 to interact with dimeric or tetrameric H3-H4 using the same interaction surface.

PubMed: 27036862
DOI: 10.1093/NAR/GKW209

Experimental method

X-RAY DIFFRACTION (4 Å)