The allosteric role of the AAA+ domain of ChlD protein from the magnesium chelatase of synechocystis species PCC 6803.
Magnesium chelatase is an AAA(+) ATPase that catalyzes the first step in chlorophyll biosynthesis, the energetically unfavorable insertion of a magnesium ion into a porphyrin ring. This enzyme contains two AAA(+) domains, one active in the ChlI protein and one inactive in the ChlD protein. Using a series of mutants in the AAA(+) domain of ChlD, we show that this site is essential for magnesium chelation and allosterically regulates Mg(2+) and MgATP(2-) binding.
From the Department of Chemistry, The University of Sheffield, Sheffield S3 7HF, United Kingdom.
Nathan B P
NB
Adams
James D
JD
Reid
D000255:Adenosine Triphosphate / Q000494:pharmacology; D000494:Allosteric Regulation; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism*; D002942:Circular Dichroism; D003905:Deuteroporphyrins / Q000378:metabolism; D007700:Kinetics; D008190:Lyases / Q000737:chemistry* / Q000378:metabolism*; D050505:Mutant Proteins / Q000737:chemistry / Q000378:metabolism; D017434:Protein Structure, Tertiary; D013329:Structure-Activity Relationship; D046939:Synechocystis / Q000201:enzymology*
D001426:Bacterial Proteins; D003905:Deuteroporphyrins; D050505:Mutant Proteins; D000255:Adenosine Triphosphate; D008190:Lyases; C086788:magnesium chelatase; C100607:ChlD protein, Synechocystis sp. PCC 6803
ATPases; Biosynthesis; Enzyme Catalysis; Mutagenesis Site-specific; Porphyrin