1UFI

Crystal structure of the dimerization domain of human CENP-B

Summary for 1UFI

• Entry DOI: 10.2210/pdb1ufi/pdb
• Descriptor: Major centromere autoantigen B (2 entities in total)
• Functional Keywords: dimerization domain, salt bridge, riken structural genomics/proteomics initiative, rsgi, structural genomics, dna binding protein
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: P07199
• Total number of polymer chains: 4
• Total formula weight: 28997.14

Authors

Tawaramoto, M.S.,Kurumizaka, H.,Tanaka, Y.,Park, S.-Y.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2003-05-30, release date: 2004-02-17, Last modification date: 2023-12-27)

Primary citation

Tawaramoto, M.S.,Park, S.-Y.,Tanaka, Y.,Nureki, O.,Kurumizaka, H.,Yokoyama, S.
Crystal structure of the human centromere protein B (CENP-B) dimerization domain at 1.65-A resolution
J.Biol.Chem., 278:51454-51461, 2003

PubMed Abstract: The human centromere protein B (CENP-B), a centromeric heterochromatin component, forms a homodimer that specifically binds to a distinct DNA sequence (the CENP-B box), which appears within every other alpha-satellite repeat. Previously, we determined the structure of the human CENP-B DNA-binding domain, CENP-B-(1-129), complexed with the CENP-B box DNA. In the present study, we determined the crystal structure of its dimerization domain (CENP-B-(540-599)), another functional domain of CENP-B, at 1.65-A resolution. CENP-B-(540-599) contains two alpha-helices, which are folded into an antiparallel configuration. The CENP-B-(540-599) dimer formed a symmetrical, antiparallel, four-helix bundle structure with a large hydrophobic patch in which 23 residues of one monomer form van der Waals contacts with the other monomer. In the CENP-B-(540-599) dimer, the N-terminal ends of CENP-B-(540-599) are oriented on opposite sides of the dimer. This CENP-B dimer configuration may be suitable for capturing two distant CENP-B boxes during centromeric heterochromatin formation.

PubMed: 14522975
DOI: 10.1074/jbc.M310388200

Experimental method

X-RAY DIFFRACTION (1.65 Å)