The tertiary structure of a bacterial cellulase determined by small-angle X-ray-scattering analysis

Biochem J. 1990 Oct 1;271(1):277-80. doi: 10.1042/bj2710277.

Abstract

CenA from Cellulomonas fimi is a beta-1,4-endoglucanase that binds tightly to cellulose. X-ray-scattering analyses show that the enzyme is tadpole-shaped: the previously identified catalytic and cellulose-binding domains comprise the head and tail respectively. It appears that this structural and functional organization is common to several cellulases from bacteria and fungi.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actinomycetales / enzymology*
  • Cellulase / chemistry*
  • Protein Conformation
  • Scattering, Radiation
  • Trichoderma / enzymology
  • X-Rays

Substances

  • Cellulase