作者: Linda B. Bloom , Myron F. Goodman
DOI: 10.1038/NSB1001-829
关键词: Protein structure 、 Chemistry 、 Biophysics 、 Dimer 、 Protein subunit 、 Clamp 、 DNA polymerase 、 DNA 、 DNA clamp 、 DNA replication
摘要: Crystal structures of the Escherichia coli DNA replication γ clamp loading complex and a subunit loader bound to β monomer provide physical framework in which view ATP-dependent modulation complex–β interactions. The structural data suggest how ring is opened loaded onto absence direct interaction between dimer interface.