Journal article
Main chain and side chain dynamics of oxidized flavodoxin from Cyanobacterium anabaena
Biochemistry (Easton), Vol.40(49), pp.14744-14753
12/11/2001
DOI: 10.1021/bi011073d
PMID: 11732893
Abstract
Oxidized flavodoxin from Cyanobacterium anabaena PCC 7119 is used as a model system to investigate the fast internal dynamics of a flavin-bearing protein. Virtually complete backbone and side chain resonance NMR assignments of an oxidized flavodoxin point mutant (C55A) have been determined. Backbone and side chain dynamics in flavodoxin (C55A) were investigated using (15)N amide and deuterium methyl NMR relaxation methods. The squared generalized order parameters (S(NH)(2)) for backbone amide N-H bonds are found to be uniformly high (<S(NH)(2)> approximately 0.923 over 109 residues in regular secondary structure), indicating considerable restriction of motion in the backbone of the protein. In contrast, methyl-bearing side chains are considerably heterogeneous in their amplitude of motion, as indicated by obtained symmetry axis squared generalized order parameters (S(axis)(2)). However, in comparison to nonprosthetic group-bearing proteins studied with these NMR relaxation methods, the side chains of oxidized flavodoxin are unusually rigid.
Details
- Title: Subtitle
- Main chain and side chain dynamics of oxidized flavodoxin from Cyanobacterium anabaena
- Creators
- Weixia Liu - The Johnson Research Foundation and Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USAPeter F FlynnErnesto J FuentesJames K KranzMargaret McCormickA. Joshua Wand
- Resource Type
- Journal article
- Publication Details
- Biochemistry (Easton), Vol.40(49), pp.14744-14753
- Publisher
- United States
- DOI
- 10.1021/bi011073d
- PMID
- 11732893
- ISSN
- 0006-2960
- eISSN
- 1520-4995
- Grant note
- GM35940 / NIGMS NIH HHS
- Language
- English
- Date published
- 12/11/2001
- Academic Unit
- Biochemistry and Molecular Biology
- Record Identifier
- 9984024533302771
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