Cloning, sequence analysis and crystal structure determination of a miraculin-like protein from Murraya koenigii

被引：23

作者：

Gahloth, Deepankar ^{[1
]}

Selvakumar, Purushotham ^{[1
]}

Shee, Chandan ^{[1
]}

Kumar, Pravindra ^{[1
]}

Sharma, Ashwani Kumar ^{[1
]}

机构：

[1] Indian Inst Technol, Dept Biotechnol, Roorkee 247667, Uttar Pradesh, India

来源：

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS | 2010年 / 494卷 / 01期

关键词：

Murraya koenigii; Cloning; Sequencing; Miraculin-like protein; Crystal structure; TRYPSIN-INHIBITOR; ERYTHRINA-CAFFRA; PORCINE TRYPSIN; KUNITZ; PURIFICATION; COMPLEX; CRYSTALLIZATION; INSIGHT; TOXIN;

D O I：

10.1016/j.abb.2009.11.008

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：

Earlier, the purification of a 21.4 kDa protein with trypsin inhibitory activity from seeds of Murraya koenigii has been reported. The present Study, based on the amino acid sequence deduced from both cDNA and genomic DNA, establishes it to be a miraculin-like protein and provides crystal structure at 2.9 angstrom resolution. The mature protein consists of 190 amino acid residues with seven cysteines arranged in three disulfide bridges. The amino acid sequence showed maximum homology and formed a distinct cluster with miraculin-like proteins, a soybean Kunitz super family member, in phylogenetic analyses. The major differences in sequence were observed at primary and secondary specificity sites in the reactive loop when compared to classical Kunitz family members. The crystal structure analysis showed that the protein is made of twelve antiparallel beta-strands, loops connecting beta-strands and two short helices. Despite similar overall fold, it showed significant differences from classical Kunitz trypsin inhibitors. (C) 2009 Elsevier Inc. All rights reserved.

引用

页码：15 / 22

页数：8

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