Neutron diffraction studies on rubredoxin from Pyrococcus furiosus.
Single-crystal neutron diffraction data up to a resolution of 1.5 A have been collected at room temperature on two forms of rubredoxin using the BIX-3 diffractometer at the JRR-3 reactor of the Japan Atomic Energy Research Institute (JAERI). Rubredoxin is a small iron-sulfur redox protein with 53 amino acid residues, and the source of this particular protein is the hyperthermophile Pyrococcus furiosus, a microorganism that normally lives at temperatures near that of boiling water. Data were collected on crystals of the wild-type protein and on a mutant in which three of the residues have been replaced. In this paper we will be describing several sets of results arising from these high-resolution neutron structure determinations: (a) the H/D exchange pattern of the N-H bonds of the main backbone, which give information about which regions of the molecule are more exposed to solvent; (b) the orientations of some of the O-D bonds in the protein, information which is often not obtainable from X-ray results; (c) the structure and appearance of water molecules in the protein crystals; and (d) some structural features which may help rationalize the remarkable thermal stability of the wild-type protein from this intriguing microorganism
Bau
Robert
R
Chemistry Department, University of Southern California, Los Angeles, CA 90007, USA.
D001665:Binding Sites; D003903:Deuterium / Q000737:chemistry; D006860:Hydrogen Bonding; D008958:Models, Molecular; D008970:Molecular Weight; D033363:Neutron Diffraction / Q000379:methods*; D011485:Protein Binding; D011487:Protein Conformation; D011489:Protein Denaturation; D017433:Protein Structure, Secondary; D020027:Pyrococcus furiosus / Q000737:chemistry*; D012416:Rubredoxins / Q000737:chemistry*; D013696:Temperature; D014867:Water / Q000737:chemistry*
D012416:Rubredoxins; D014867:Water; D003903:Deuterium