1ix0

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I59A-3SS human lysozyme

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

This study sought to attain a better understanding of the contribution of, buried water molecules to protein stability. The 3SS human lysozyme lacks, one disulfide bond between Cys77 and Cys95 and is significantly, destabilized compared with the wild-type human lysozyme (4SS). We examined, the structure and stability of the I59A-3SS mutant human lysozyme, in, which a cavity is created at the mutation site. The crystal structure of, I59A-3SS indicated that there were ordered new water molecules in the, cavity created. The stability of I59A-3SS is 5.5 kJ/mol less than that of, 3SS. The decreased stability of I59A-3SS (5.5 kJ/mol) is similar to that, of Ile to Ala mutants with newly introduced water molecules in other, globular proteins (6.3 +/- 2.1 kJ/mol), but is less than that of Ile/Leu, to Ala mutants with empty cavities (13.7 +/- 3.1 kJ/mol). This indicates, that water molecules partially compensate for the destabilization by, decreasing hydrophobic and van der Waals interactions. These results, provide further evidence that buried water molecules contribute to protein, stability.

Disease

Known diseases associated with this structure: Amyloidosis, renal OMIM:[153450], Microphthalmia, syndromic 1 OMIM:[309800]

About this Structure

1IX0 is a Single protein structure of sequence from Homo sapiens with as ligand. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.

Reference

Buried water molecules contribute to the conformational stability of a protein., Takano K, Yamagata Y, Yutani K, Protein Eng. 2003 Jan;16(1):5-9. PMID:12646687

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