7mdh
From Proteopedia
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| - | | | + | {{STRUCTURE_7mdh| PDB=7mdh | SCENE= }} |
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'''STRUCTURAL BASIS FOR LIGHT ACITVATION OF A CHLOROPLAST ENZYME. THE STRUCTURE OF SORGHUM NADP-MALATE DEHYDROGENASE IN ITS OXIDIZED FORM''' | '''STRUCTURAL BASIS FOR LIGHT ACITVATION OF A CHLOROPLAST ENZYME. THE STRUCTURE OF SORGHUM NADP-MALATE DEHYDROGENASE IN ITS OXIDIZED FORM''' | ||
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==Reference== | ==Reference== | ||
Structural basis for light activation of a chloroplast enzyme: the structure of sorghum NADP-malate dehydrogenase in its oxidized form., Johansson K, Ramaswamy S, Saarinen M, Lemaire-Chamley M, Issakidis-Bourguet E, Miginiac-Maslow M, Eklund H, Biochemistry. 1999 Apr 6;38(14):4319-26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10194350 10194350] | Structural basis for light activation of a chloroplast enzyme: the structure of sorghum NADP-malate dehydrogenase in its oxidized form., Johansson K, Ramaswamy S, Saarinen M, Lemaire-Chamley M, Issakidis-Bourguet E, Miginiac-Maslow M, Eklund H, Biochemistry. 1999 Apr 6;38(14):4319-26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10194350 10194350] | ||
| - | [[Category: Malate dehydrogenase (NADP(+))]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Sorghum bicolor]] | [[Category: Sorghum bicolor]] | ||
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[[Category: Ramaswamy, S.]] | [[Category: Ramaswamy, S.]] | ||
[[Category: Saarinen, M.]] | [[Category: Saarinen, M.]] | ||
| - | [[Category: | + | [[Category: Activated by light]] |
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Revision as of 19:46, 4 May 2008
STRUCTURAL BASIS FOR LIGHT ACITVATION OF A CHLOROPLAST ENZYME. THE STRUCTURE OF SORGHUM NADP-MALATE DEHYDROGENASE IN ITS OXIDIZED FORM
Overview
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.
About this Structure
7MDH is a Single protein structure of sequence from Sorghum bicolor. Full crystallographic information is available from OCA.
Reference
Structural basis for light activation of a chloroplast enzyme: the structure of sorghum NADP-malate dehydrogenase in its oxidized form., Johansson K, Ramaswamy S, Saarinen M, Lemaire-Chamley M, Issakidis-Bourguet E, Miginiac-Maslow M, Eklund H, Biochemistry. 1999 Apr 6;38(14):4319-26. PMID:10194350 Page seeded by OCA on Sun May 4 22:46:38 2008
