The three-dimensional structure of sperm whale myoglobin His64(E7)-->Val,Thr67(E10)-->Arg double mutant has been studied by X-ray crystallography at 1.6 angstrom resolution, and refined to a crystallographic R-factor of 0.197. The Arg67(E10) side chain is extended in the direction of the ligand binding site, and its NH1 atom is at a distance of 3.11 angstrom from the NH1 atom of Arg45(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.
Crystal structure of a distal site double mutant of sperm whale myoglobin at 1.6 A resolution / Rizzi, M; Bolognesi, M; Coda, A; Cutruzzola', Francesca; TRAVAGLINI ALLOCATELLI, Carlo; Brancaccio, A; Brunori, Maurizio. - In: FEBS LETTERS. - ISSN 0014-5793. - 320:1(1993), pp. 13-16. [10.1016/0014-5793(93)81647-I]
Crystal structure of a distal site double mutant of sperm whale myoglobin at 1.6 A resolution.
CUTRUZZOLA', Francesca;TRAVAGLINI ALLOCATELLI, Carlo;BRUNORI, Maurizio
1993
Abstract
The three-dimensional structure of sperm whale myoglobin His64(E7)-->Val,Thr67(E10)-->Arg double mutant has been studied by X-ray crystallography at 1.6 angstrom resolution, and refined to a crystallographic R-factor of 0.197. The Arg67(E10) side chain is extended in the direction of the ligand binding site, and its NH1 atom is at a distance of 3.11 angstrom from the NH1 atom of Arg45(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.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
