Crystallization and preliminary crystallographic study of the functional form of the Bacillus thuringiensis mosquito-larvicidal Cry4Aa mutant toxin

被引：9

作者：

Boonserm, P

Angsuthanasombat, C

Lescar, J

机构：

[1] Mahidol Univ, Inst Mol Biol & Genet, Nakhon Pathom 73170, Thailand

[2] Nanyang Technol Univ, Sch Biol Sci, Singapore 637551, Singapore

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2004年 / 60卷

关键词：

D O I：

10.1107/S0907444904011205

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

The 65 kDa functional form of the mosquito-larvicidal Cry4Aa-R235Q mutant toxin has been crystallized. The crystals belong to space group C222(1), with unit-cell parameters a = 91.2, b = 202.1, c = 98.7 Angstrom, and contain one molecule per asymmetric unit. The crystals diffract to similar to2.9 Angstrom using synchrotron radiation and a complete native data set has been collected. The structure has been solved using a molecular-replacement method with the Cry4Ba toxin protein as a search model.

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页码：1315 / 1318

页数：4

相关论文

共 33 条

[1] Introduction of Culex toxicity into Bacillus thuringiensis Cry4Ba by protein engineering [J].

Abdullah, MAF ;

Alzate, O ;

Mohammad, M ;

McNall, RJ ;

Adang, MJ ;

Dean, DH .

APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 2003, 69 (09) :5343-5353

[2]

ANGSUTHANASOMBAT C, 1993, FEMS MICROBIOL LETT, V111, P255

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

BAILEY, S .

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

[4] Optimised expression in Escherichia coli and purification of the functional form of the Bacillus thuringiensis Cry4Aa δ-endotoxin [J].

Boonserm, P ;

Pornwiroon, W ;

Katzenmeier, G ;

Panyim, S ;

Angsuthanasombat, C .

PROTEIN EXPRESSION AND PURIFICATION, 2004, 35 (02) :397-403

[5] Crystallization and preliminary X-ray diffraction studies of a mosquito-larvicidal toxin from Bacillus thuringiensis subsp israelensis [J].

Boonserm, P ;

Ellar, DJ ;

Li, JD .

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 2003, 59 :591-594

[6]

Brunger AT, 1998, ACTA CRYSTALLOGR D, V54, P905, DOI 10.1107/s0907444998003254

[7] N-acetylgalactosamine on the putative insect receptor aminopeptidase N is recognised by a site on the domain III lectin-like fold of a Bacillus thuringiensis insecticidal toxin [J].

Burton, SL ;

Ellar, DJ ;

Li, J ;

Derbyshire, DJ .

JOURNAL OF MOLECULAR BIOLOGY, 1999, 287 (05) :1011-1022

[8] SITE-DIRECTED MUTATIONS IN A HIGHLY CONSERVED REGION OF BACILLUS-THURINGIENSIS DELTA-ENDOTOXIN AFFECT INHIBITION OF SHORT-CIRCUIT CURRENT ACROSS BOMBYX-MORI MIDGUTS [J].

CHEN, XJ ;

LEE, MK ;

DEAN, DH .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1993, 90 (19) :9041-9045

[9] Revision of the nomenclature for the Bacillus thuringiensis pesticidal crystal proteins [J].

Crickmore, N ;

Zeigler, DR ;

Feitelson, J ;

Schnepf, E ;

Van Rie, J ;

Lereclus, D ;

Baum, J ;

Dean, DH .

MICROBIOLOGY AND MOLECULAR BIOLOGY REVIEWS, 1998, 62 (03) :807-+

[10] Structure of the insecticidal bacterial δ-endotoxin Cry3Bb1 of Bacillus thuringiensis [J].

Galitsky, N ;

Cody, V ;

Wojtczak, A ;

Ghosh, D ;

Luft, JR ;

Pangborn, W ;

English, L .

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 2001, 57 :1101-1109

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