REFINED STRUCTURE OF CYTOCHROME B(562) FROM ESCHERICHIA-COLI AT 1.4 ANGSTROM RESOLUTION

被引:66
作者
HAMADA, K [1 ]
BETHGE, PH [1 ]
MATHEWS, FS [1 ]
机构
[1] WASHINGTON UNIV,SCH MED,DEPT BIOCHEM & MOLEC BIOPHYS,ST LOUIS,MO 63110
关键词
CYTOCHROME; CRYSTALLOGRAPHY; ELECTRON TRANSFER; HEME; REFINEMENT;
D O I
10.1006/jmbi.1995.0192
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 structure of cytochrome b(562) from Escherichia Coli has been refined at 1.4 Angstrom resolution against X-ray data collected on a Picker four-circle diffractometer. The triclinic unit cell parameters are a = 33.68 Angstrom b = 50.48 Angstrom, c = 32.67 Angstrom, alpha = 102.51 degrees, beta = 86.56 degrees and gamma = 107.01 degrees and there are two molecules in the asymmetric unit. A total of 138 cycles of restrained crystallographic refinement using the program PROLSQ were augmented at intermediate stages by two cycles of simulated annealing refinement using X-PLOR. The final crystallographic R-factor is 16.4% for data in the resolution range 6.0 Angstrom to 1.4 Angstrom for a model containing 1650 protein atoms, 86 heme atoms, 165 water molecules and four sulfate anions. The root-mean-square deviations from ideal bond lengths and angles are 0.012 Angstrom and 2.0 degrees, respectively Each molecule consists of a bundle of four alpha-helices arranged in a simple up-down-up-down manner With a non-covalently bound heme group inserted between the first and fourth helices. In addition, there is a very short 3(10) helix in the 15-residue loop connecting the first and second pairs of helices. The two independent molecules show r.m.s. differences of 0.30 Angstrom for main-chain atoms and 0.88 Angstrom for all atoms. A detailed comparison with the structurally similar cytochrome c' from Rhodospirulum molishianum is presented. in addition, the titration behavior of cytochrome b(562) in solution is discussed in terms of its molecular structure.
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页码:947 / 962
页数:16
相关论文
共 48 条
[21]  
Lederer F., Glatigny A., Bethge P.H., Bellamy H.D., Mathews F.S., Improvement of the 2.5 Å resolution model of cytochrome b<sub>562</sub> by redetermining the primary structure and using molecular graphics, J. Mol. Biol., 148, pp. 427-448, (1981)
[22]  
Lewis P.N., Momany F.A., Scheraga H.A., Chain reversals in proteins, Biochim. Biophys. Acta, 303, pp. 211-229, (1973)
[23]  
Louie G.V., Brayer G.D., High-resolution refinement of yeast iso-1-cytochrome c and comparisons with other eukaryotic cytochromes c, J. Mol. Biol., 214, pp. 527-555, (1990)
[24]  
Luzzati V., Traitement statistique des erreurs dans la determination des structures crystallines, Acta. Crystallogr., 5, pp. 802-810, (1952)
[25]  
Mathews F.S., The structure, function and evolution of cytochromes, Prog. Biophys. Mol. Biol., 45, pp. 1-56, (1985)
[26]  
Mathews F.S., Bethge P.H., Czerwinski E.W., The structure of cytochrome b<sub>562</sub> from Escherichia coli at 2.5 Å resolution, J. Biol. Chem., 254, pp. 1699-1706, (1979)
[27]  
Matsuura Y., Takano T., Dickerson R.E., Structure of cytochrome c<sub>551</sub> from Pseudomonas aeruginosa refined at 1.6 Å resolution and comparison of the two redox forms, J. Mol. Biol., 156, pp. 389-410, (1982)
[28]  
McGregor M.J., Islam S.A., Sternberg M.J.E., Analysis of the relationship between side-chain conformation and secondary structure in globular proteins, J. Mol. Biol., 198, pp. 295-310, (1987)
[29]  
Meyer T.E., Kamen M.D., New perspectives on c-type cytochromes, Advan. Protein Chem., 35, pp. 105-212, (1982)
[30]  
Moore G.R., Williams R.J.P., Peterson J., Thomson A.J., Mathews F.S., A spectroscopic investigation of the structure and redox properties of Escherichia coli cytochrome b<sub>562</sub>, Biochim. Biophys. Acta, 829, pp. 83-96, (1985)