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

FEBS Letters

Coda, Alessandro¹  Rizzi, Menico¹  Brancaccio, Andrea²  Cutruzzolà, Francesca²  Brunori, Maurizio²  Bolognesi, Martino¹  Allocatelli, Carlo Travaglini² 

[1] Dipartimento di Genetica e Microbiologia, Centro Interuniversitario Studio Macromolecole Informazionali, Università di Pavia, Via Abbiategrasso 207, 27100 Pavia, Italy;Dipartimento di Scienze Biochimiche ‘A. Rossi Fanelli’ e Centro di Biologia Molecolare del CNR Università di Roma ‘La Sapienza’, P. le A. Moro 5, 00185 Roma, Italy

关键词: Protein engineering;    Myoglobin mutant;    Ligand binding;    NMR;    nuclear magnetic resonance;    V mutant;    HiS64(E7)→Val sperm whale myoglobin single mutant;    VR mutant;    HiS64(E7)→Val;    Thr67(E10)→Arg sperm whale myoglobin double mutant;    Mb;    myoglobin;    rms;    root mean square;    Rsym. merging R-factor between symmetry related reflections:where Ihis 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 [1] within the conventional globin fold;   

DOI  :  10.1016/0014-5793(93)81647-I

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The three-dimensional structure of sperm whale myoglobin His⁶⁴(E7)→Val,Thr⁶⁴(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 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 Å 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.

【 授权许可】

Unknown