PDBsum entry 3zc8

Hydrolase inhibitor

PDB id: 3zc8

Contents

Protein chain

182 a.a.

Waters ×76

PDB id:

3zc8

Name:

Hydrolase inhibitor

Title:

Crystal structure of murraya koenigii miraculin-like protein at 2.2 a resolution at ph 7.0

Structure:

Trypsin inhibitor. Chain: a. Synonym: miraculin-like protein

Source:

Murraya koenigii. Curry leaf. Organism_taxid: 311449. Organ: seeds

Resolution:

2.24Å R-factor: 0.195 R-free: 0.242

Authors:

P.Selvakumar,N.Sharma,P.P.S.Tomar,P.Kumar,A.K.Sharma

Key ref:

P.Selvakumar et al. (2014). Structural insights into the aggregation behavior of Murraya koenigii miraculin-like protein below pH 7.5. Proteins, 82, 830-840. PubMed id: 24265134 DOI: 10.1002/prot.24461

Date:

19-Nov-12 Release date: 04-Dec-13

Protein chain

D2YW43  (D2YW43_MURKO) -  Trypsin inhibitor from Murraya koenigii

Seq: 190 a.a.

Struc: 182 a.a.

DOI no: 10.1002/prot.24461

Proteins 82:830-840 (2014)

PubMed id: 24265134

Structural insights into the aggregation behavior of Murraya koenigii miraculin-like protein below pH 7.5.

P.Selvakumar, N.Sharma, P.P.Tomar, P.Kumar, A.K.Sharma.

ABSTRACT

Murraya koenigii miraculin-like protein (MKMLP) gradually precipitates below pH 7.5. Here, we explore the basis for this aggregation by identifying the aggregation-prone regions via comparative analysis of crystal structures acquired at several pH values. The prediction of aggregation-prone regions showed the presence of four short peptides either in beta sheets or loops on surface of the protein. These peptides were distributed in two patches far apart on the surface. Comparison of crystal structures of MKMLP, determined at 2.2 Å resolution in pH 7.0 and 4.6 in the present study and determined at 2.9 Å in pH 8.0 in an earlier reported study, reveal subtle conformational differences resulting in gradual exposure of aggregation-prone regions. As the pH is lowered, there are alterations in ionic interactions within the protein interactions of the chain with water molecules and exposure of hydrophobic residues. The analysis of symmetry-related molecular interfaces involving one patch revealed shortening of nonpolar intermolecular contacts as the pH decreased. In particular, a decrease in the intermolecular distance between Trp103 of the aggregation-prone peptide WFITTG (103-108) unique to MLPs was observed. These results demonstrated that aggregation occurs due to the cumulative effect of the changes in interactions in two aggregation-prone defined regions. Proteins 2014; 82:830-840. © 2013 Wiley Periodicals, Inc.