New mechanistic insights from structural studies of the oxygen-sensing domain of Bradyrhizobium japonicum FixL

被引:131
作者
Gong, WM
Hao, B
Chan, MK
机构
[1] Ohio State Univ, Dept Biochem, Columbus, OH 43210 USA
[2] Ohio State Univ, Dept Chem, Columbus, OH 43210 USA
关键词
D O I
10.1021/bi992346w
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 FixL heme domain serves as the dioxygen switch in the FixL/FixJ two-component system of Rhizobia. Recent structural studies of the Bradyrhizobium japonicum FixL heme domain (BjFixLH) have suggested an allosteric mechanism that is distinct from the classical hemoglobin model. To gain further insight into the FixL sensing mechanism, structures of BjFixLH bound to dioxygen, imidazole, and nitric oxide have been determined. These structures, particularly the structure of BjFixLH bound to its physiological ligand, dioxygen, have helped to address a number of important issues relevant to the BjFixLH sensing mechanism. On the basis of the oxy-BjFixLH structure, a conserved arginine is found to stabilize the dioxygen ligand in a mode reminiscent of the distal histidine in classical myoglobins and hemoglobins. The structure of BjFixLH bound to imidazole elucidates the structural requirements for accommodating sterically bulky ligands, Finally, the structure of BjFixLH bound to nitric oxide provides evidence for a structural intermediate in the heme-driven conformational change.
引用
收藏
页码:3955 / 3962
页数:8
相关论文
共 34 条
[1]   OXYGEN REGULATION OF NIFA TRANSCRIPTION INVITRO [J].
AGRON, PG ;
DITTA, GS ;
HELINSKI, DR .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1993, 90 (08) :3506-3510
[2]   CRYSTAL-STRUCTURE OF ASIAN ELEPHANT (ELEPHAS-MAXIMUS) CYANO-METMYOGLOBIN AT 1.78-ANGSTROM RESOLUTION - PHE(29)(B10) ACCOUNTS FOR ITS UNUSUAL LIGAND-BINDING PROPERTIES [J].
BISIG, DA ;
DIIORIO, EE ;
DIEDERICHS, K ;
WINTERHALTER, KH ;
PIONTEK, K .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1995, 270 (35) :20754-20762
[3]  
BRUNNETT B, 1993, SURVEYS MATH IND, V3, P1
[4]   DETECTION OF A NITROUS-OXIDE REDUCTASE STRUCTURAL GENE IN RHIZOBIUM-MELILOTI STRAINS AND ITS LOCATION ON THE NOD MEGAPLASMID OF JJ1C10 AND SU47 [J].
CHAN, YK ;
WHEATCROFT, R .
JOURNAL OF BACTERIOLOGY, 1993, 175 (01) :19-26
[5]   X-RAY CRYSTAL-STRUCTURE OF FERRIC APLYSIA-LIMACINA MYOGLOBIN IN DIFFERENT LIGANDED STATES [J].
CONTI, E ;
MOSER, C ;
RIZZI, M ;
MATTEVI, A ;
LIONETTI, C ;
CODA, A ;
ASCENZI, P ;
BRUNORI, M ;
BOLOGNESI, M .
JOURNAL OF MOLECULAR BIOLOGY, 1993, 233 (03) :498-508
[6]   Nitric oxide binding to the ferri- and ferroheme states of nitrophorin 1, a reversible NO-binding heme protein from the saliva of the blood-sucking insect, Rhodnius prolixus [J].
Ding, XD ;
Weichsel, A ;
Andersen, JF ;
Shokhireva, TK ;
Balfour, C ;
Pierik, AJ ;
Averill, BA ;
Montfort, WR ;
Walker, FA .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1999, 121 (01) :128-138
[7]   Synthesis, molecular structures, and properties of six-coordinate [Fe(OEP)(L)(NO)] plus derivatives: Elusive nitrosyl ferric porphyrins [J].
Ellison, MK ;
Scheidt, WR .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1999, 121 (22) :5210-5219
[8]   Structural distortion in five-coordinate nitrosyl iron porphyrins. Axial ligand tilting and its effect on equatorial geometry [J].
Ellison, MK ;
Scheidt, WR .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1997, 119 (31) :7404-7405
[9]   HEME-BASED SENSORS, EXEMPLIFIED BY THE KINASE FIXL, ARE A NEW CLASS OF HEME PROTEIN WITH DISTINCTIVE LIGAND-BINDING AND AUTOXIDATION [J].
GILLESGONZALEZ, MA ;
GONZALEZ, G ;
PERUTZ, MF ;
KIGER, L ;
MARDEN, MC ;
POYART, C .
BIOCHEMISTRY, 1994, 33 (26) :8067-8073
[10]   KINASE-ACTIVITY OF OXYGEN SENSOR FIXL DEPENDS ON THE SPIN-STATE OF ITS HEME IRON [J].
GILLESGONZALEZ, MA ;
GONZALEZ, G ;
PERUTZ, MF .
BIOCHEMISTRY, 1995, 34 (01) :232-236