Article
N1,N1-Diethyl-N 2-(2,3,4,6-tetra-O-acetyl-β-D-glucopyranosyl)acetamidine
Author/s | Diánez Millán, María Jesús
Estrada de Oya, María Dolores López Castro, Amparo Pérez Garrido, Simeón |
Department | Universidad de Sevilla. Departamento de Física de la Materia Condensada |
Publication Date | 2001 |
Deposit Date | 2017-04-03 |
Published in |
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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 ... 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 ¯exible in solution and that this ¯exibility may be important for receptor recognition. Sequence comparisons are used to identify regions of the sequence unique to the cyanobacteria |
Citation | Diánez Millán, M.J., Estrada de Oya, M.D., López Castro, A. y Pérez Garrido, S. (2001). N1,N1-Diethyl-N 2-(2,3,4,6-tetra-O-acetyl-β-D-glucopyranosyl)acetamidine. Acta Crystallographica Section C: Crystal Structure Communications, 57 (11), 2183-2190. |
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The structures of the PII.pdf | 1.069Mb | [PDF] | View/ | |