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| {{STRUCTURE_2o66| PDB=2o66 | SCENE= }} | | {{STRUCTURE_2o66| PDB=2o66 | SCENE= }} |
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| '''Crystal Structure of Arabidopsis thaliana PII bound to citrate'''
| | ===Crystal Structure of Arabidopsis thaliana PII bound to citrate=== |
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| ==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. | | The line below this paragraph, {{ABSTRACT_PUBMED_17279613}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17279613 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17279613}} |
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| ==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]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 10:22:35 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 16:35:52 2008'' |