1rsm
From Proteopedia
THE 2-ANGSTROMS RESOLUTION STRUCTURE OF A THERMOSTABLE RIBONUCLEASE A CHEMICALLY CROSS-LINKED BETWEEN LYSINE RESIDUES 7 AND 41
Overview
The crystal structure of Lys-7-(dinitrophenylene)-Lys-41-cross-linked ribonuclease A has been determined by molecular replacement and refined by restrained least-squares methods to an R factor of 0.18 at 2.0-A resolution. Diffraction intensity data were collected by using a conventional diffractometer and an x-ray area detector. Comparison of the thermostable cross-linked protein and the native enzyme shows them to be structurally similar, with a rms difference in backbone and side-chain atoms of 0.52 and 1.34 A, respectively. Native and modified proteins additionally show 35 common bound solvent sites and similar overall temperature factor behavior, despite localized differences resulting from cross-link introduction, altered crystal pH, or lattice interactions with neighboring molecules. These results are discussed in the context of proposals on the origins of thermostability in the cross-linked enzyme.
About this Structure
1RSM is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
The 2-A resolution structure of a thermostable ribonuclease A chemically cross-linked between lysine residues 7 and 41., Weber PC, Sheriff S, Ohlendorf DH, Finzel BC, Salemme FR, Proc Natl Acad Sci U S A. 1985 Dec;82(24):8473-7. PMID:3936036 Page seeded by OCA on Sat May 3 07:51:32 2008
