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1k3f

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(New page: 200px<br /><applet load="1k3f" size="450" color="white" frame="true" align="right" spinBox="true" caption="1k3f, resolution 2.5&Aring;" /> '''Uridine Phosphorylase...)
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Revision as of 16:42, 20 November 2007


1k3f, resolution 2.5Å

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Uridine Phosphorylase from E. coli, Refined in the Monoclinic Crystal Lattice

Overview

Uridine phosphorylase from E. coli (Upase) has been crystallized using, vapor diffusion technique in a new monoclinic crystal form. The structure, was determined by the molecular replacement method at 2.5 A resolution., The coordinates of the trigonal crystal form were used as a starting model, and the refinement by the program XPLOR led to the R-factor of 18.6%. The, amino acid fold of the protein was found to be the same as that in the, trigonal crystals. The positions of flexible regions were refined. The, conclusion about the involvement in the active site is in good agreement, with the results of the biochemical experiments.

About this Structure

1K3F is a Single protein structure of sequence from Escherichia coli. Active as Uridine phosphorylase, with EC number 2.4.2.3 Full crystallographic information is available from OCA.

Reference

Atomic structure at 2.5 A resolution of uridine phosphorylase from E. coli as refined in the monoclinic crystal lattice., Morgunova EYu, Mikhailov AM, Popov AN, Blagova EV, Smirnova EA, Vainshtein BK, Mao C, Armstrong ShR, Ealick SE, Komissarov AA, et al., FEBS Lett. 1995 Jun 26;367(2):183-7. PMID:7796917

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