Trimeric domain-swapped barnase

被引：49

作者：

Zegers, I ^{[1
]}

Deswarte, J ^{[1
]}

Wyns, L ^{[1
]}

机构：

[1] Free Univ Brussels VIB, Lab Ultrastruct, B-1640 Rhode St Genese, Belgium

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1999年 / 96卷 / 03期

关键词：

protein folding; trimerization;

D O I：

10.1073/pnas.96.3.818

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The structure of a trimeric domain-swapped form of barnase (EC 3.1.27.3) was determined by x-ray crystallography at a resolution of 2.2 Angstrom from crystals of space group R32. Residues 1-36 of one molecule associate with residues 41-110 from another molecule related through three-fold symmetry. The resulting cyclic trimer contains three protein folds that are very similar to those in monomeric barnase. Both swapped domains contain a nucleation site for folding. The formation of a domain-swapped trimer is consistent with the description of the folding process of monomeric barnase as the formation and subsequent association of two foldons.

引用

页码：818 / 822

页数：5

共 25 条

[1] A COMPARISON OF THE PH, UREA, AND TEMPERATURE-DENATURED STATES OF BARNASE BY HETERONUCLEAR NMR - IMPLICATIONS FOR THE INITIATION OF PROTEIN-FOLDING [J].

ARCUS, VL ;

VUILLEUMIER, S ;

FREUND, SMV ;

BYCROFT, M ;

FERSHT, AR .

JOURNAL OF MOLECULAR BIOLOGY, 1995, 254 (02) :305-321

[2] THE CCP4 SUITE - PROGRAMS FOR PROTEIN CRYSTALLOGRAPHY [J].

BAILEY, S .

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 1994, 50 :760-763

[3]

BRUNGER AT, 1992, XPLOR VERSION 3 1 SY

[4] SUBSITE BINDING IN AN RNASE - STRUCTURE OF A BARNASE TETRANUCLEOTIDE COMPLEX AT 1.76-ANGSTROM RESOLUTION [J].

BUCKLE, AM ;

FERSHT, AR .

BIOCHEMISTRY, 1994, 33 (07) :1644-1653

[5] Folding intermediates of wild-type and mutants of barnase.: I.: Use of φ-value analysis and m-values to probe the cooperative nature of the folding pre-equilibrium [J].

Dalby, PA ;

Oliveberg, M ;

Fersht, AR .

JOURNAL OF MOLECULAR BIOLOGY, 1998, 276 (03) :625-646

[6] An extensively modified version of MolScript that includes greatly enhanced coloring capabilities [J].

Esnouf, RM .

JOURNAL OF MOLECULAR GRAPHICS & MODELLING, 1997, 15 (02) :132-+

[7] PROTEIN-FOLDING AND STABILITY - THE PATHWAY OF FOLDING OF BARNASE [J].

FERSHT, AR .

FEBS LETTERS, 1993, 325 (1-2) :5-16

[8] Nucleation mechanisms in protein folding [J].

Fersht, AR .

CURRENT OPINION IN STRUCTURAL BIOLOGY, 1997, 7 (01) :3-9

[9] Initiation sites of protein folding by NMR analysis [J].

Freund, SMV ;

Wong, KB ;

Fersht, AR .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1996, 93 (20) :10600-10603

[10] SURFACE, SUBUNIT INTERFACES AND INTERIOR OF OLIGOMERIC PROTEINS [J].

JANIN, J ;

MILLER, S ;

CHOTHIA, C .

JOURNAL OF MOLECULAR BIOLOGY, 1988, 204 (01) :155-164

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