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. 1990 Oct 1;271(1):277–280. doi: 10.1042/bj2710277

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

I Pilz 1, E Schwarz 1, D G Kilburn 1, R C Miller Jr 1, R A Warren 1, N R Gilkes 1
PMCID: PMC1149546  PMID: 2121133

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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