Crystal structure of a distal site double mutant of sperm whale myoglobin at 1.6 Å resolution

The three-dimensional structure of sperm whale myoglobin His 64(E7)→Val,Thr 64(E10)→Arg double mutant has been studied by X-ray crystallography at 1.6 Å resolution, and refined to a crystallographic R-factor of 0.197. The Arg 67(E10) side chain is extended in the direction of the ligand binding site...

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Veröffentlicht in:	FEBS letters 1993-03, Vol.320 (1), p.13-16
Hauptverfasser:	Rizzi, Menico, Bolognesi, Martino, Coda, Alessandro, Cutruzzolà, Francesca, Allocatelli, Carlo Travaglini, Brancaccio, Andrea, Brunori, Maurizio
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Binding Sites Biological and medical sciences Crystalline structure Fundamental and applied biological sciences. Psychology Ligand binding Mb, myoglobin Molecular biophysics Mutation Myoglobin - chemistry Myoglobin - genetics Myoglobin mutant NMR, nuclear magnetic resonance Protein Conformation Protein engineering R sym. merging R-factor between symmetry related reflections: where I h is the observed intensity of the j-th measurement of reflection h, and < I h> is its mean value. Amino acid residues have been identified by their three-letter codes, sequence number and topological position within the conventional globin fold rms, root mean square Rsym. merging R-factor between symmetry related reflections: where Ih is the observed intensity of the j-th measurement of reflection h, and is its mean value. Amino acid residues have been identified by their three-letter codes, sequence number and topological position within the conventional globin fold Structure in molecular biology V mutant, HiS 64(E7)→Val sperm whale myoglobin single mutant V mutant, HiS64(E7)→Val sperm whale myoglobin single mutant VR mutant, HiS 64(E7)→Val,Thr 67(E10)→Arg sperm whale myoglobin double mutant VR mutant, HiS64(E7)→Val,Thr67(E10)→Arg sperm whale myoglobin double mutant Whales X-Ray Diffraction
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Zusammenfassung:	The three-dimensional structure of sperm whale myoglobin His 64(E7)→Val,Thr 64(E10)→Arg double mutant has been studied by X-ray crystallography at 1.6 Å resolution, and refined to a crystallographic R-factor of 0.197. The Arg 67(E10) side chain is extended in the direction of the ligand binding site, and its NH1 atom is at a distance of 3.11 Å from the NH1 atom of Arg 45(CD3), which is also pointing towards the distal site. Both are kept in this position by hydrogen bonding and electrostatic interactions with a solvent sulfate ion, located amongst the two, on the protein surface. No liganded water molecule is present at the sixth coordination position of the Fe(III) heme.
ISSN:	0014-5793 1873-3468
DOI:	10.1016/0014-5793(93)81647-I