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 Lettjournal_title
FEBS lettersauthors
Sundström M,Lindqvist Y,Schneider Gdoi
10.1016/0014-5793(92)81197-tkeywords:
subject
Has Abstractpub_date
1992-11-30 00:00:00pages
229-31issue
3eissn
0014-5793issn
1873-3468pii
0014-5793(92)81197-Tjournal_volume
313pub_type
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