2J46

Water structure of T. Aquaticus Ffh NG Domain At 1.1A Resolution

Summary for 2J46

• Entry DOI: 10.2210/pdb2j46/pdb
• Related: 1FFH 1JPJ 1JPN 1LS1 1NG1 1O87 1OKK 1RJ9 1RY1 2C03 2C04 2CNW 2FFH 2J45 2NG1 3NG1
• Descriptor: SIGNAL RECOGNITION PARTICLE PROTEIN, (4R)-2-METHYLPENTANE-2,4-DIOL, CHLORIDE ION, ... (6 entities in total)
• Functional Keywords: ribonucleoprotein, nucleotide-binding, srp, ffh, water, gtpase, rna-binding, gtp-binding, signal recognition particle
• Biological source: THERMUS AQUATICUS
• Total number of polymer chains: 2
• Total formula weight: 65749.40

Authors

Freymann, D.M.,Ramirez, U.D. (deposition date: 2006-08-24, release date: 2006-11-30, Last modification date: 2023-12-13)

Primary citation

Ramirez, U.D.,Freymann, D.M.
Analysis of Protein Hydration in Ultra-High Resolution Structures of the Srp Gtpase Ffh
Acta Crystallogr.,Sect.D, 62:1520-, 2006

PubMed Abstract: Two new structures of the SRP GTPase Ffh have been determined at 1.1 A resolution and provide the basis for comparative examination of the extensive water structure of the apo conformation of these GTPases. A set of well defined water-binding positions have been identified in the active site of the two-domain ;NG' GTPase, as well as at two functionally important interfaces. The water hydrogen-bonding network accommodates alternate conformations of the protein side chains by undergoing local rearrangements and, in one case, illustrates binding of a solute molecule within the active site by displacement of water molecules without further disruption of the water-interaction network. A subset of the water positions are well defined in several lower resolution structures, including those of different nucleotide-binding states; these appear to function in maintaining the protein structure. Consistent arrangements of surface water between three different ultrahigh-resolution structures provide a framework for beginning to understand how local water structure contributes to protein-ligand and protein-protein binding in the SRP GTPases.

PubMed: 17139088
DOI: 10.1107/S0907444906040807

Experimental method

X-RAY DIFFRACTION (1.14 Å)