2o67
From Proteopedia
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Crystal structure of Arabidopsis thaliana PII bound to malonate
Overview
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.
About this Structure
2O67 is a Single protein structure of sequence from Arabidopsis thaliana with as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of Arabidopsis PII reveals novel structural elements unique to plants., Mizuno Y, Berenger B, Moorhead GB, Ng KK, Biochemistry. 2007 Feb 13;46(6):1477-83. PMID:17279613
Page seeded by OCA on Thu Feb 21 18:15:01 2008
