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

M Rizzi; M Bolognesi; A Coda; F Cutruzzolà; C T Allocatelli; A Brancaccio; M Brunori

doi:10.1016/0014-5793(93)81647-i

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

FEBS Lett. 1993 Mar 29;320(1):13-6. doi: 10.1016/0014-5793(93)81647-i.

Authors

M Rizzi¹, M Bolognesi, A Coda, F Cutruzzolà, C T Allocatelli, A Brancaccio, M Brunori

Affiliation

¹ Dipartimento di Genetica e Microbiologia, Università di Pavia, Italy.

PMID: 8462669
DOI: 10.1016/0014-5793(93)81647-i

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 A 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 A 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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Animals
Binding Sites
Mutation
Myoglobin / chemistry*
Myoglobin / genetics
Protein Conformation
Whales
X-Ray Diffraction

Substances

Myoglobin