Three-dimensional structure of apotransketolase. Flexible loops at the active site enable cofactor binding.

Abstract:

:The structure determination of apotransketolase and the comparison of its three-dimensional structure with that of the holoenzyme has revealed that no large conformational changes are associated with cofactor binding. Two loops at the active site are flexible in the apoenzyme which enables ThDP to reach its binding site. Binding of the cofactor induces defined conformations for these two loops at the active site. One of these loops is directly involving in binding of the cofactors, Ca2+ and ThDP. This loop acts like a flap which closes off the diphosphate binding site. After binding of the cofactor, residues of this loop form interactions to residues of loop 383-398 from the second subunit. These interactions stabilize the conformation of the two loops from a flexible to a 'closed' conformation.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Sundström M,Lindqvist Y,Schneider G

doi

10.1016/0014-5793(92)81197-t

keywords:

subject

Has Abstract

pub_date

1992-11-30 00:00:00

pages

229-31

issue

3

eissn

0014-5793

issn

1873-3468

pii

0014-5793(92)81197-T

journal_volume

313

pub_type

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