5HH7

crystal structure of Arabidopsis ORC1b BAH-PHD cassette in complex with unmodified H3 peptide

Summary for 5HH7

• Entry DOI: 10.2210/pdb5hh7/pdb
• Descriptor: Origin of replication complex subunit 1B, Histone H3 1-15 peptide, ZINC ION, ... (4 entities in total)
• Functional Keywords: phd finger, bah domain, multivalent readout, transcription
• Biological source: Arabidopsis thaliana (Mouse-ear cress); More
• Cellular location: Nucleus : Q9SU24
• Total number of polymer chains: 2
• Total formula weight: 29097.67

Authors

Li, S.,Du, J. (deposition date: 2016-01-10, release date: 2016-03-09, Last modification date: 2024-03-20)

Primary citation

Li, S.,Yang, Z.,Du, X.,Liu, R.,Wilkinson, A.W.,Gozani, O.,Jacobsen, S.E.,Patel, D.J.,Du, J.
Structural Basis for the Unique Multivalent Readout of Unmodified H3 Tail by Arabidopsis ORC1b BAH-PHD Cassette
Structure, 24:486-494, 2016

PubMed Abstract: DNA replication initiation relies on the formation of the origin recognition complex (ORC). The plant ORC subunit 1 (ORC1) protein possesses a conserved N-terminal BAH domain with an embedded plant-specific PHD finger, whose function may be potentially regulated by an epigenetic mechanism. Here, we report structural and biochemical studies on the Arabidopsis thaliana ORC1b BAH-PHD cassette which specifically recognizes the unmodified H3 tail. The crystal structure of ORC1b BAH-PHD cassette in complex with an H3(1-15) peptide reveals a strict requirement for the unmodified state of R2, T3, and K4 on the H3 tail and a novel multivalent BAH and PHD readout mode for H3 peptide recognition. Such recognition may contribute to epigenetic regulation of the initiation of DNA replication.

PubMed: 26876097
DOI: 10.1016/j.str.2016.01.004

Experimental method

X-RAY DIFFRACTION (1.901 Å)