PDBsum entry 3iir

Hydrolase inhibitor

PDB id: 3iir

Contents

Protein chains

190 a.a. *

Waters ×69

* Residue conservation analysis

PDB id:

3iir

Name:

Hydrolase inhibitor

Title:

Crystal structure of miraculin like protein from seeds of murraya koenigii

Structure:

Trypsin inhibitor. Chain: a, b. Fragment: unp residues 26-215. Synonym: miraculin like protein

Source:

Murraya koenigii. Organism_taxid: 311449. Other_details: seeds

Resolution:

2.90Å R-factor: 0.220 R-free: 0.295

Authors:

D.Gahloth,P.Selvakumar,C.Shee,P.Kumar,A.K.Sharma

Key ref:

D.Gahloth et al. (2010). Cloning, sequence analysis and crystal structure determination of a miraculin-like protein from Murraya koenigii. Arch Biochem Biophys, 494, 15-22. PubMed id: 19914199

Date:

03-Aug-09 Release date: 08-Dec-09

Protein chains

D2YW43  (D2YW43_MURKO) -  Trypsin inhibitor from Murraya koenigii

Seq: 190 a.a.

Struc: 190 a.a.

Arch Biochem Biophys 494:15-22 (2010)

PubMed id: 19914199

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

D.Gahloth, P.Selvakumar, C.Shee, P.Kumar, A.K.Sharma.

ABSTRACT

Earlier, the purification of a 21.4kDa 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 2.9A 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.