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Functional implications of structural differences between variants A and B of bovine beta-lactoglobulin.

Authors
  • Qin, B Y
  • Bewley, M C
  • Creamer, L K
  • Baker, E N
  • Jameson, G B
Type
Published Article
Journal
Protein science : a publication of the Protein Society
Publication Date
Jan 01, 1999
Volume
8
Issue
1
Pages
75–83
Identifiers
PMID: 10210185
Source
Medline
License
Unknown

Abstract

The structure of the trigonal crystal form of bovine beta-lactoglobulin variant B at pH 7.1 has been determined by X-ray diffraction methods at a resolution of 2.22 A and refined to values for R and Rfree of 0.239 and 0.286, respectively. By comparison with the structure of the trigonal crystal form of bovine beta-lactoglobulin variant A at pH 7.1, which was determined previously [Qin BY et al., 1998, Biochemistry 37:14014-14023], the structural consequences of the sequence differences D64G and V118A of variants A and B, respectively, have been investigated. Only minor differences in the core calyx structure occur. In the vicinity of the mutation site D64G on loop CD (residues 61-67), there are small changes in main-chain conformation, whereas the substitution V118A on beta-strand H is unaccompanied by changes in the surrounding structure, thereby creating a void volume and weakened hydrophobic interactions with a consequent loss of thermal stability relative to variant A. A conformational difference is found for the loop EF, implicated in the pH-dependent conformational change known as the Tanford transition, but it is not clear whether this reflects differences intrinsic to the variants in solution or differences in crystallization.

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