3bu4
From Proteopedia
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RIBONUCLEASE T1 COMPLEX WITH 2'GMP
Overview
We systematically analyzed the crystallographically determined water, molecules of all known structures of RNase T1 and compared them to the, ordered solvent in a large number of related microbial nucleases. To, assess the crystallographers' impact on the interpretation of the solvent, structure, we independently refined five validation structures from, diffraction data derived from five isomorphous crystals of RNase T1. We, also compared the positions of water molecules found in 11 published, isomorphous RNase T1 inhibitor complexes. These data suggest that the, positions of most of the waters located on the surface of a protein and, that are well-determined in the experimental electron density maps are, determined primarily by crystal packing forces. Water molecules with less, well-defined electron density are in general unique to one or a small, number of crystal structures. Only a small number of the well-defined, waters are found to be independent of the crystal environment. These, waters have a low accessible surface area and B-factor, and tend to be, conserved in the crystal structures of a number of evolutionary related, ribonucleases as well. A single water molecule is found conserved in all, known microbial ribonucleases.
About this Structure
3BU4 is a Single protein structure of sequence from Aspergillus oryzae with CA and 2GP as ligands. Active as Ribonuclease T(1), with EC number 3.1.27.3 Full crystallographic information is available from OCA.
Reference
Conserved water molecules in a large family of microbial ribonucleases., Loris R, Langhorst U, De Vos S, Decanniere K, Bouckaert J, Maes D, Transue TR, Steyaert J, Proteins. 1999 Jul 1;36(1):117-34. PMID:10373011
Page seeded by OCA on Tue Nov 20 19:31:30 2007
