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1qy7

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1qy7, resolution 2.0Å

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The structure of the PII protein from the cyanobacteria Synechococcus sp. PCC 7942

Overview

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.

About this Structure

1QY7 is a Single protein structure of sequence from Synechococcus sp. with SO4 and NI as ligands. Full crystallographic information is available from OCA.

Reference

The structures of the PII proteins from the cyanobacteria Synechococcus sp. PCC 7942 and Synechocystis sp. PCC 6803., Xu Y, Carr PD, Clancy P, Garcia-Dominguez M, Forchhammer K, Florencio F, Vasudevan SG, Tandeau de Marsac N, Ollis DL, Acta Crystallogr D Biol Crystallogr. 2003 Dec;59(Pt 12):2183-90. Epub 2003, Nov 27. PMID:14646076

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