SOLUTION STRUCTURE OF APOCYTOCHROME B(562)

被引：134

作者：

FENG, YQ ^{[1
]}

SLIGAR, SG ^{[1
]}

WAND, AJ ^{[1
]}

机构：

[1] UNIV ILLINOIS,DEPT BIOCHEM,ROGER ADAMS LAB 415,URBANA,IL 61801

来源：

NATURE STRUCTURAL BIOLOGY | 1994年 / 1卷 / 01期

关键词：

D O I：

10.1038/nsb0194-30

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 apoprotein is an important intermediate on the folding pathways of many haem proteins, yet a detailed structure of such an intermediate has remained elusive. Here we present the structure of apocytochrome b(562) obtained by NMR spectroscopy. The apoprotein has a topology similar to the holoprotein. Nevertheless, significant differences in helix-helix packing between the two are evident. Much of the haem binding pocket in the apoprotein is preserved but exposed to solvent creating a large cavern. As apocytochrome b(562) displays many of the physical characteristics ascribed to the molten globule state, these results help ellucidate the origin of several properties of the protein molten globule.

引用

页码：30 / 35

页数：6

共 42 条

[1]

BALDWIN RL, 1991, CHEMTRACTS BIOCH MOL, V2, P379

[2] THE MOLTEN GLOBULE INTERMEDIATE OF APOMYOGLOBIN AND THE PROCESS OF PROTEIN FOLDING [J].

BARRICK, D ;

BALDWIN, RL .

PROTEIN SCIENCE, 1993, 2 (06) :869-876

[3] CHARACTERIZATION OF A PARTLY FOLDED PROTEIN BY NMR METHODS - STUDIES ON THE MOLTEN GLOBULE STATE OF GUINEA-PIG ALPHA-LACTALBUMIN [J].

BAUM, J ;

DOBSON, CM ;

EVANS, PA ;

HANLEY, C .

BIOCHEMISTRY, 1989, 28 (01) :7-13

[4] 3-DIMENSIONAL STRUCTURE OF PROTEINS DETERMINED BY MOLECULAR-DYNAMICS WITH INTERPROTON DISTANCE RESTRAINTS - APPLICATION TO CRAMBIN [J].

BRUNGER, AT ;

CLORE, GM ;

GRONENBORN, AM ;

KARPLUS, M .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1986, 83 (11) :3801-3805

[5] RIBBON MODELS OF MACROMOLECULES [J].

CARSON, M .

JOURNAL OF MOLECULAR GRAPHICS, 1987, 5 (02) :103-&

[6]

CHYAN CL, 1992, BIOCHEMISTRY-US, V29, P5681

[7] 2-DIMENSIONAL, 3-DIMENSIONAL, AND 4-DIMENSIONAL NMR METHODS FOR OBTAINING LARGER AND MORE PRECISE 3-DIMENSIONAL STRUCTURES OF PROTEINS IN SOLUTION [J].

CLORE, GM ;

GRONENBORN, AM .

ANNUAL REVIEW OF BIOPHYSICS AND BIOPHYSICAL CHEMISTRY, 1991, 20 :29-63

[8] STRUCTURAL COMPARISON OF APOMYOGLOBIN AND METAQUOMYOGLOBIN - PH TITRATION OF HISTIDINES BY NMR-SPECTROSCOPY [J].

COCCO, MJ ;

KAO, YH ;

PHILLIPS, AT ;

LECOMTE, JTJ .

BIOCHEMISTRY, 1992, 31 (28) :6481-6491

[9] CHARACTERIZATION OF HYDROPHOBIC CORES IN APOMYOGLOBIN - A PROTON NMR-SPECTROSCOPY STUDY [J].

COCCO, MJ ;

LECOMTE, JTJ .

BIOCHEMISTRY, 1990, 29 (50) :11067-11072

[10] THE DISULFIDE FOLDING PATHWAY OF BPTI [J].

CREIGHTON, TE .

SCIENCE, 1992, 256 (5053) :111-112

← 1 2 3 4 5 →