Five Glutamic Acid Residues in the C-Terminal Domain of the ChlD Subunit Play a Major Role in Conferring Mg2+ Cooperativity upon Magnesium Chelatase | Zendy

Amanda A. Brindley | Zendy; Nathan B. P. Adams | Zendy; C. Neil Hunter | Zendy; J. David Reid | Zendy

Open Access

Five Glutamic Acid Residues in the C-Terminal Domain of the ChlD Subunit Play a Major Role in Conferring Mg²⁺ Cooperativity upon Magnesium Chelatase

Author(s) -

Amanda A. Brindley,

Nathan B. P. Adams,

C. Neil Hunter,

J. David Reid

Publication year - 2015

Publication title -

biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.43

H-Index - 253

eISSN - 1520-4995

pISSN - 0006-2960

DOI - 10.1021/acs.biochem.5b01080

Subject(s) - cooperativity , chemistry , synechocystis , c terminus , biochemistry , protein subunit , glutamic acid , stereochemistry , amino acid , mutant , gene

Magnesium chelatase catalyzes the first committed step in chlorophyll biosynthesis by inserting a Mg(2+) ion into protoporphyrin IX in an ATP-dependent manner. The cyanobacterial (Synechocystis) and higher-plant chelatases exhibit a complex cooperative response to free magnesium, while the chelatases from Thermosynechococcus elongatus and photosynthetic bacteria do not. To investigate the basis for this cooperativity, we constructed a series of chimeric ChlD proteins using N-terminal, central, and C-terminal domains from Synechocystis and Thermosynechococcus. We show that five glutamic acid residues in the C-terminal domain play a major role in this process.

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