Crystallization and preliminary X-ray crystallographic investigations on a βγ-crystallin domain of absent in melanoma 1 (AIM1), a protein from Homo sapiens

被引：3

作者：

Aravind, P ^{[1
]}

Rajini, B ^{[1
]}

Sharma, Y ^{[1
]}

Sankaranarayanan, R ^{[1
]}

机构：

[1] Ctr Cellular & Mol Biol, Hyderabad 500007, Andhra Pradesh, India

来源：

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2006年 / 62卷

基金：

英国惠康基金;

关键词：

D O I：

10.1107/S1744309106005380

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

AIM1g1 is a single beta gamma-crystallin domain from the protein absent in melanoma 1 (AIM1), which appears to play a role in the suppression of melanomas. This domain is known to bind calcium and its structure would help in identifying calcium-coordinating sites in vertebrate crystallins, which have hitherto been believed to have lost this ability during evolution. Crystallization of this domain was performed by the hanging-drop vapour-diffusion method. Crystals diffracted to a maximum resolution of 1.86 angstrom and were found to belong to space group P6(1) or P6(5), with unit-cell parameters a = b = 54.98, c = 59.73 angstrom. Solvent-content analysis indicated the presence of one monomer per asymmetric unit.

引用

页码：282 / 284

页数：3

共 17 条

[1]

Bhat SP, 2003, PROG DRUG RES, V60, P205

[2] Crystal structure of the calcium-loaded spherulin 3a dimer sheds light on the evolution of the eye lens βγ-crystallin domain fold [J].

Clout, NJ ;

Kretschmar, M ;

Jaenicke, R ;

Slingsby, C .

STRUCTURE, 2001, 9 (02) :115-124

[3] EVOLUTION OF EYE LENS CRYSTALLINS - THE STRESS CONNECTION [J].

DEJONG, WW ;

HENDRIKS, W ;

MULDERS, JWM ;

BLOEMENDAL, H .

TRENDS IN BIOCHEMICAL SCIENCES, 1989, 14 (09) :365-368

[4] Preparation and characterization of geodin -: A βγ-crystallin-type protein from a sponge [J].

Giancola, C ;

Pizzo, E ;

Di Maro, A ;

Cubellis, MV ;

D'Alessio, G .

FEBS JOURNAL, 2005, 272 (04) :1023-1035

[5] Lens crystallins and their microbial homologs: Structure, stability, and function [J].

Jaenicke, R ;

Slingsby, C .

CRITICAL REVIEWS IN BIOCHEMISTRY AND MOLECULAR BIOLOGY, 2001, 36 (05) :435-499

[6] Calcium-binding crystallins from Yersinia pestis -: Characterization of two single βγ-crystallin domains of a putative exported protein [J].

Jobby, MK ;

Sharma, Y .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2005, 280 (02) :1209-1216

[7] NMR structure of Streptomyces killer toxin-like protein, SKLP:: Further evidence for the wide distribution of single-domain βγ-crystallin superfamily proteins [J].

Ohki, S ;

Kariya, E ;

Hiraga, K ;

Wakamiya, A ;

Isobe, T ;

Oda, K ;

Kainosho, M .

JOURNAL OF MOLECULAR BIOLOGY, 2001, 305 (01) :109-120

[8] Processing of X-ray diffraction data collected in oscillation mode [J].

Otwinowski, Z ;

Minor, W .

MACROMOLECULAR CRYSTALLOGRAPHY, PT A, 1997, 276 :307-326

[9] Stability, homodimerization, and calcium-binding properties of a single, variant βγ-crystallin domain of the protein absent in melanoma 1 (AIM1) [J].

Rajini, B ;

Graham, C ;

Wistow, G ;

Sharma, Y .

BIOCHEMISTRY, 2003, 42 (15) :4552-4559

[10] Calcium binding properties of γ-crystallin -: Calcium ion binds at the Greek key βγ-crystallin fold [J].

Rajini, B ;

Shridas, P ;

Sundari, CS ;

Muralidhar, D ;

Chandani, S ;

Thomas, F ;

Sharma, Y .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (42) :38464-38471

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