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1rsm
From Proteopedia
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(New page: 200px<br /><applet load="1rsm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rsm, resolution 2.0Å" /> '''THE 2-ANGSTROMS RESOL...)
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Revision as of 23:43, 20 November 2007
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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 with NIN as ligand. Active as Pancreatic ribonuclease, with EC number 3.1.27.5 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
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