The structures of the PII proteins from the cyanobacteria Synechococcus sp. PCC 7942 and Synechocystis sp. PCC 6803

Yibin Xu, Paul D. Carr, Paula Clancy, Mario Garcia-Dominguez, Karl Forchhammer, Francisco Florencio, Nicole Tandeau De Marsac, Subhash G. Vasudevan, David L. Ollis*

*Corresponding author for this work

    Research output: Contribution to journalArticlepeer-review

    46 Citations (Scopus)

    Abstract

    The PII proteins from the cyanobacteria Synechococcus sp. PCC 7942 and Synechocystis sp. PCC 6803 have been crystallized and high-resolution structures have been obtained using X-ray crystallography. The core of these new structures is similar to that of the PII proteins from Escherichia coli, although the structures of the T- and C-loops differ. The T-loop of the Synechococcus protein is ordered, but appears to be stabilized by crystal contacts. The same loop in the Synechocystis protein is disordered. The C-terminus of the Synechocystis protein is stabilized by hydrogen bonding to the same region of a crystallographically related molecule. The same terminus in the Synechococcus protein is stabilized by coordination with a metal ion. These observations are consistent with the idea that both the T-loop and the C-terminus of PII proteins are flexible in solution and that this flexibility may be important for receptor recognition. Sequence comparisons are used to identify regions of the sequence unique to the cyanobacteria.

    Original languageEnglish
    Pages (from-to)2183-2190
    Number of pages8
    JournalActa Crystallographica Section D: Structural Biology
    Volume59
    Issue number12
    DOIs
    Publication statusPublished - Dec 2003

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