The structure of the PII-ATP complex

Xu, Yibin, Carr, Paul D., Huber, Thomas, Vasudevan, Subhash G., and Ollis, David L. (2001) The structure of the PII-ATP complex. European Journal of Biochemistry, 268 (7). pp. 2028-2037.

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P II is a signal transduction protein that is part of the cellular machinery used by many bacteria to regulate the activity of glutamine synthetase and the transcription of its gene. The structure of P II was solved using a hexagonal crystal form (form I). The more physiologically relevant form of P II is a complex with small molecule effectors. We describe the structure of PII with ATP obtained by analysis of two different crystal forms (forms II and III) that were obtained by co-crystallization of P II with ATP. Both structures have a disordered recognition (T) loop and show differences at their C termini. Comparison of these structures with the form I protein reveals changes that occur on binding ATP. Surprisingly, the structure of the P II/ATP complex differs with that of GlnK, a functional homologue. The two proteins bind the base and sugar of ATP in a similar manner but show differences in the way that they interact with the phosphates. The differences in structure could account for the differences in their activities, and these have been attributed to a difference in sequence at position 82. It has been demonstrated recently that P II and GlnK form functional heterotrimers in vivo. We construct models of the heterotrimers and examine the junction between the subunits.

Item ID: 13205
Item Type: Article (Research - C1)
ISSN: 1742-4658
Keywords: ATP binding protein; GlnK; signal transduction; x-ray structure
Date Deposited: 30 Jul 2012 04:48
FoR Codes: 06 BIOLOGICAL SCIENCES > 0601 Biochemistry and Cell Biology > 060199 Biochemistry and Cell Biology not elsewhere classified @ 100%
SEO Codes: 82 PLANT PRODUCTION AND PLANT PRIMARY PRODUCTS > 8299 Other Plant Production and Plant Primary Products > 829999 Plant Production and Plant Primary Products not elsewhere classified @ 100%
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