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

• 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; http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=A1993KU54100004&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=0c7ff228ccbaaa74236f48834a34396a; http://www.scopus.com/inward/record.url?eid=2-s2.0-0027537610&partnerID=65&md5=37cbdd9ce0b54311f34d16ec41f40d6f

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.