CRYSTAL-STRUCTURE OF A DISTAL SITE DOUBLE MUTANT OF SPERM WHALE MYOGLOBIN AT 1.6 ANGSTROM RESOLUTION

被引：12

作者：

RIZZI, M

BOLOGNESI, M

CODA, A

CUTRUZZOLA, F

ALLOCATELLI, CT

BRANCACCIO, A

BRUNORI, M

机构：

[1] UNIV GENOA,IST,BIOSTRUCT GRP,I-16132 GENOA,ITALY

[2] UNIV ROMA LA SAPIENZA,CNR,DIPARTIMENTO SCI BIOCHIM A ROSSI FANELLI,I-00185 ROME,ITALY

[3] UNIV ROMA LA SAPIENZA,CNR,CTR BIOL MOLEC,I-00185 ROME,ITALY

来源：

FEBS LETTERS | 1993年 / 320卷 / 01期

关键词：

PROTEIN ENGINEERING; MYOGLOBIN MUTANT; LIGAND BINDING;

D O I：

10.1016/0014-5793(93)81647-I

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：13 / 16

页数：4

共 20 条

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