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

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 ligan...

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Bibliographic Details
Published in:FEBS Letters
Main Authors: Rizzi M, Bolognesi M, Coda A, Brancaccio A, CUTRUZZOLA', Francesca, TRAVAGLINI ALLOCATELLI, Carlo, BRUNORI, Maurizio
Other Authors: Rizzi, M, Bolognesi, M, Coda, A, Cutruzzola', Francesca, Brancaccio, A, Brunori, Maurizio
Format: Article in Journal/Newspaper
Language:English
Published: ELSEVIER SCIENCE BV, PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS 1993
Subjects:
Sperm whale
Online Access:http://hdl.handle.net/11573/406627
https://doi.org/10.1016/0014-5793(93)81647-I
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Summary: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.

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