2O67

Crystal structure of Arabidopsis thaliana PII bound to malonate

Summary for 2O67

• Entry DOI: 10.2210/pdb2o67/pdb
• Related: 2O66
• Descriptor: PII protein, MALONATE ION (3 entities in total)
• Functional Keywords: regulation of nitrogen and carbon metabolism, biosynthetic protein
• Biological source: Arabidopsis thaliana (thale cress)
• Cellular location: Plastid, chloroplast: Q9ZST4
• Total number of polymer chains: 3
• Total formula weight: 44645.88

Authors

Mizuno, Y.M.,Berenger, B.,Moorhead, G.B.G.,Ng, K.K.S. (deposition date: 2006-12-06, release date: 2007-02-20, Last modification date: 2023-08-30)

Primary citation

Mizuno, Y.,Berenger, B.,Moorhead, G.B.,Ng, K.K.
Crystal Structure of Arabidopsis PII Reveals Novel Structural Elements Unique to Plants.
Biochemistry, 46:1477-1483, 2007

PubMed Abstract: The 1.9 A resolution crystal structure of PII from Arabidopsis thaliana reveals for the first time the molecular structure of a widely conserved regulator of carbon and nitrogen metabolism from a eukaryote. The structure provides a framework for understanding the arrangement of highly conserved residues shared with PII proteins from bacteria, archaea, and red algae as well as residues conserved only in plant PII. Most strikingly, a highly conserved segment at the N-terminus that is found only in plant PII forms numerous interactions with the alpha2 helix and projects from the surface of the homotrimer opposite to that occupied by the T-loop. In addition, solvent-exposed residues near the T-loop are highly conserved in plants but differ in prokaryotes. Several residues at the C-terminus that are also highly conserved only in plants contribute part of the ATP-binding site and likely participate in an ATP-induced conformational change. Structures of PII also reveal how citrate and malonate bind near the triphosphate binding site occupied by ATP in bacterial and archaeal PII proteins.

PubMed: 17279613
DOI: 10.1021/bi062149e

Experimental method

X-RAY DIFFRACTION (2.5 Å)