High-Resolution Structure of the Soluble, Respiratory-Type Rieske Protein from Thermus thermophilus: Analysis and Comparison

The structure of the soluble Rieske protein from Thermus thermophilus has been determined at a resolution of 1.3 Å at pH 8.5 using multiwavelength anomalous dispersion (MAD) techniques. This is the first report of a Rieske protein from a menaquinone-utilizing organism. The structure shows an overall...

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Veröffentlicht in:	Biochemistry 2003-06, Vol.42 (24), p.7303-7317
Hauptverfasser:	Hunsicker-Wang, Laura M, Heine, Andreas, Chen, Ying, Luna, Eugene P, Todaro, Thomas, Zhang, Yan Ming, Williams, Pamela A, McRee, Duncan E, Hirst, Judy, Stout, C. David, Fee, James A
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Crystallography, X-Ray - methods Electron Transport Complex III Hydrogen Bonding Iron-Sulfur Proteins - analysis Iron-Sulfur Proteins - chemistry Iron-Sulfur Proteins - genetics Iron-Sulfur Proteins - metabolism Models, Molecular Molecular Sequence Data PARTICLE ACCELERATORS Probability Protein Binding Protein Structure, Secondary Protein Structure, Tertiary PROTEINS Sequence Homology, Amino Acid Solubility STANFORD LINEAR ACCELERATOR CENTER STANFORD SYNCHROTRON RADIATION LABORATORY Static Electricity SYNCHROTRON RADIATION Thermus thermophilus - chemistry
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