1SMN

IDENTIFICATION OF THE SERRATIA ENDONUCLEASE DIMER: STRUCTURAL BASIS AND IMPLICATIONS FOR CATALYSIS

1SMN の概要

• エントリーDOI: 10.2210/pdb1smn/pdb
• 分子名称: EXTRACELLULAR ENDONUCLEASE (2 entities in total)
• 機能のキーワード: nuclease, dnase, rnase, sugar-nonspecific nuclease, endonuclease
• 由来する生物種: Serratia marcescens
• 細胞内の位置: Secreted: P13717
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 53477.79

構造登録者

Miller, M.D.,Krause, K.L. (登録日: 1995-01-25, 公開日: 1996-01-29, 最終更新日: 2024-10-23)

主引用文献

Miller, M.D.,Krause, K.L.
Identification of the Serratia endonuclease dimer: structural basis and implications for catalysis.
Protein Sci., 5:24-33, 1996

PubMed Abstract: The Serratia endonuclease is an extracellularly secreted enzyme capable of cleaving both single- and double-stranded forms of DNA and RNA. It is the first member of a large class of related and usually dimeric endonucleases for which a structure is known. Using X-ray crystallography, the structure of monomer of this enzyme was reported by us previously (Miller MD et al., 1994, Nature Struct Biol 1:461-468). We now confirm the dimeric nature of this enzyme through light-scattering experiments and identify the physiologic dimer interface through crystal packing analysis. This dimerization occurs through an isologous twofold interaction localized to the carboxy-terminal subdomain of the enzyme. The dimer is a prolate ellipsoid with dimensions 30 A x 35 A x 90 A. The dimer interface is flat and contains four salt links, several hydrogen bonds, and nonpolar interactions. Buried water is prominent in this interface and it includes an unusual "cubic" water cluster. The position of the two active sites in the dimer suggests that they can act independently in their cleavage of DNA, but have a geometrical advantage in attacking substrate relative to the monomer.

PubMed: 8771193

実験手法

X-RAY DIFFRACTION (2.04 Å)