Abstract：
:Some key chloroplast enzymes are activated by light via a ferredoxin-thioredoxin reduction system which reduces disulfide bridges in the enzymes. We describe for the first time the structural basis for the redox activation of a chloroplast enzyme, the NADP-dependent malate dehydrogenase (MDH) from Sorghum vulgare whose structure has been determined and refined at 2.4 A resolution. In addition to the normal structural components of MDHs, the enzyme exhibits extensions at both the N- and C-termini, each of which contains a regulatory disulfide bridge which must be reduced for activation. The N-terminal disulfide motif is inserted in a cleft between the two subunits of the dimer, thereby locking the domains in each subunit. The C-terminal disulfide keeps the C-terminal residues tight to the enzyme surface and blocks access to the active site. Reduction of the N-terminal disulfide would release the stopper between the domains and give the enzyme the necessary flexibility. Simultaneous reduction of the C-terminal disulfide would free the C-terminal residues from binding to the enzyme and make the active site accessible.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Johansson K,Ramaswamy S,Saarinen M,Lemaire-Chamley M,Issakidis-Bourguet E,Miginiac-Maslow M,Eklund Hdoi
10.1021/bi982876csubject
Has Abstractpub_date
1999-04-06 00:00:00pages
4319-26issue
14eissn
0006-2960issn
1520-4995pii
bi982876cjournal_volume
38pub_type
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