1aqb

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Revision as of 08:55, 20 November 2007

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spinqualitylabelsall models 1aqb, resolution 1.65Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

RETINOL-BINDING PROTEIN (RBP) FROM PIG PLASMA

Overview

The crystal structure of pig plasma retinol-binding protein (RBP) has been, determined at 1.65 A resolution. The space group is P212121, with a =, 45.81 (4), b = 53.14 (5), c = 72.97 (8) A and one protein molecule in the, asymmetric unit. The structure has been solved using the molecular, replacement method and refined with restrained least squares to an R, factor of 0.1844 and an Rfree of 0.237 for 18 874 and 1001 independent, reflections, respectively. The relatively high resolution structure of pig, holoRBP has revealed some new structural details. Moreover, it has, provided a description of the binding site for Cd2+, a metal ion which is, required for protein crystallization. The hepta-coordination of the, RBP-bound cadmium ion involves different residues of two symmetry-related, RBP molecules, consistent with the participation of the cation in, intermolecular interactions that in turn promote protein crystallization.

About this Structure

1AQB is a Single protein structure of sequence from Sus scrofa domestica with CD and RTL as ligands. Full crystallographic information is available from OCA.

Reference

Structure of pig plasma retinol-binding protein at 1.65 A resolution., Zanotti G, Panzalorto M, Marcato A, Malpeli G, Folli C, Berni R, Acta Crystallogr D Biol Crystallogr. 1998 Sep 1;54(Pt 5):1049-52. PMID:9757135

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