2o66: Difference between revisions

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[[Image:2o66.jpg|left|200px]]
{{Seed}}
[[Image:2o66.png|left|200px]]


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{{STRUCTURE_2o66|  PDB=2o66  |  SCENE=  }}  
{{STRUCTURE_2o66|  PDB=2o66  |  SCENE=  }}  


'''Crystal Structure of Arabidopsis thaliana PII bound to citrate'''
===Crystal Structure of Arabidopsis thaliana PII bound to citrate===




==Overview==
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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.
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{{ABSTRACT_PUBMED_17279613}}


==About this Structure==
==About this Structure==
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[[Category: Ng, K K.S.]]
[[Category: Ng, K K.S.]]
[[Category: Regulation of nitrogen and carbon metabolism]]
[[Category: Regulation of nitrogen and carbon metabolism]]
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