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Structural changes in cellobiohydrolase I upon binding of a macromolecular ligand as evident by SAXS investigations.

Abstract：

:Xylan from Rhodymenia palmata binds to the cellobiohydrolase I from Trichoderma reesei (CBH I) or its core protein, inhibiting their activity. Adsorption onto microcrystalline cellulose (Avicel) is reduced approximately 30% for intact CBH I and nearly 50% for the core, whereas the effects with cellobiose are negligible. Structural changes concomitant with this binding are studied in solution by small angle X-ray scattering. In the "tadpole" structure typical for the CBH I [Abuja et al., 1988] the lengthening of the tail part is the most salient observation when xylan is present which accounts for an increase in Dmax (18.0 to 22.0 nm) and radius of gyration (4.74 to 5.18 nm). When xylan binds to the core the radius of gyration remains nearly unchanged. Here a model can be constructed showing a xylan molecule on the surface of the core protein near the tail part.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Abuja PM,Pilz I,Tomme P,Claeyssens M

doi

10.1016/s0006-291x(89)80010-5

subject

Has Abstract

pub_date

1989-12-15 00:00:00

pages

615-23

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(89)80010-5

journal_volume

165

pub_type

杂志文章

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