title: The tertiary structure of a bacterial cellulase determined by small-angle X-ray-scattering analysis.
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.
authors.affiliation: Institut für Physikalische Chemie, Universität Graz, Austria.
authors.forename: I
authors.initials: I
authors.lastname: Pilz
authors.forename: E
authors.initials: E
authors.lastname: Schwarz
authors.forename: D G
authors.initials: DG
authors.lastname: Kilburn
authors.forename: R C
authors.initials: RC
authors.lastname: Miller
authors.forename: R A
authors.initials: RA
authors.lastname: Warren
authors.forename: N R
authors.initials: NR
authors.lastname: Gilkes
mesh_terms: D000192:Actinomycetales / Q000201:enzymology*; D002480:Cellulase / Q000737:chemistry*; D011487:Protein Conformation; D012542:Scattering, Radiation; D014242:Trichoderma / Q000201:enzymology; D014965:X-Rays
chemical_list: D002480:Cellulase