Work

Refined crystal structure of ytterbium‐substituted carp parvalbumin 4.25 at 1.5 Å, and its comparison with the native and cadmium‐substituted structures

Year: 1991

Type: article

Abstract: The crystal structure of carp parvalbumin 4.25 containing a 1:1 molar ratio of ytterbium chloride to protein has been refined at 1.5 A resolution by restrained least-squares methods to a crystallographic R value of 0.199. The crystal structure confirms the NMR studies, which suggest that low concentrations of ytterbium cause an extensive displacement of calcium from the EF metal binding site. A comparison of the ytterbium-substituted model with the native and cadmium-substituted structure show no significant differences, except around the substituted EF metal-binding region. The displacement of calcium by ytterbium at the EF site has caused a movement in the polypeptide backbone of Ser-91 and Asp-92. This movement resulted in an increase in the number of oxygen ligands bound to ytterbium in the EF site from seven to eight.

Source: FEBS Letters

DOI: 10.1016/0014-5793(91)80616-b

Authors: Vinod D. Kumar, Lana Lee, Brian F.P. Edwards

Institutions: Frederick National Laboratory for Cancer Research, National Cancer Institute, University of Windsor, Wayne State University

Language: English

Topic: Enzyme Structure and Function

Subfield: Structural Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: bronze

Funders: National Institutes of Health, National Cancer Institute, National Institute of General Medical Sciences, National Center for Research Resources

Awards: BASIC RESEARCH--CANCER INSTITUTE FREDERICK, G225764842, GRAPHICS SYSTEM FOR MODELING MOLECULES AND SURFACES, STRUCTURAL STUDIES ON PROTEINS INVOLVED IN HEMOSTASIS