Research Article

Anabaena apoflavodoxin hydrogen exchange: On the stable exchange core of the α/β(21345) flavodoxin-like family

  1. Grant M. Langdon1,3,
  2. M. Angeles Jiménez1,
  3. Carlos G. Genzor2,4,
  4. Susana Maldonado2,
  5. Javier Sancho2,
  6. Manuel Rico1,*

Article first published online: 16 APR 2001

DOI: 10.1002/prot.1059

Issue

Proteins: Structure, Function, and Bioinformatics

Proteins: Structure, Function, and Bioinformatics

Volume 43, Issue 4, pages 476–488, 1 June 2001

Additional Information

How to Cite

Langdon, G. M., Jiménez, M. A., Genzor, C. G., Maldonado, S., Sancho, J. and Rico, M. (2001), Anabaena apoflavodoxin hydrogen exchange: On the stable exchange core of the α/β(21345) flavodoxin-like family. Proteins: Structure, Function, and Bioinformatics, 43: 476–488. doi: 10.1002/prot.1059

Author Information

  1. 1

    Instituto de Estructura de la Materia, C.S.I.C., Madrid, Spain

  2. 2

    Departamento de Bioquímica y Biología Molecular y Celular, Facultad de Ciencias, Universidad de Zaragoza, Zaragoza, Spain

  3. 3

    Proteinstrukturfabrik, Institute of Molecular Pharmacology, Berlin, Germany

  4. 4

    OPERON S.A. Camino del Plano 19, Zaragoza, Spain

*Instituto de Estructura de la Materia, C.S.I.C. Serrano 119, 28006-Madrid, Spain

Publication History

  1. Issue published online: 16 APR 2001
  2. Article first published online: 16 APR 2001
  3. Manuscript Accepted: 27 FEB 2001
  4. Manuscript Received: 11 AUG 2000

Funded by

  • Spanish DGYCT. Grant Number: PB 98-0677
  • DGES, Spain. Grant Number: PB97-1027
  • CONSI+D, DGA, Spain. Grant Number: P15/97

SEARCH

SEARCH BY CITATION

ARTICLE TOOLS

View Full Article (HTML) Get PDF (414K)

Keywords:

  • flavodoxin-like;
  • protein stability;
  • protein folding;
  • hydrogen/deuterium exchange;
  • nuclear magnetic resonance

Abstract

An important issue in modern protein biophysics is whether structurally homologous proteins share common stability and/or folding features. Flavodoxin is an archetypal α/β protein organized in three layers: a central β-sheet (strand order 21345) flanked by helices 1 and 5 on one side and helices 2, 3, and 4 on the opposite side. The backbone internal dynamics of the apoflavodoxin from Anabaena is analyzed here by the hydrogen exchange method. The hydrogen exchange rates indicate that 46 amide protons, distributed throughout the structure of apoflavodoxin, exchange relatively slowly at pH 7.0 (kex < 10−1 min−1). According to their distribution in the structure, protein stability is highest on the β-sheet, helix 4, and on the layer formed by helices 1 and 5. The exchange kinetics of Anabaena apoflavodoxin was compared with those of the apoflavodoxin from Azotobacter, with which it shares a 48% sequence identity, and with Che Y and cutinase, two other α/β (21345) proteins with no significant sequence homology with flavodoxins. Both similarities and differences are observed in the cores of these proteins. It is of interest that a cluster of a few structurally equivalent residues in the central β-strands and in helix 5 is common to the cores. Proteins 2001;43:476–488. © 2001 Wiley-Liss, Inc.

View Full Article (HTML) Get PDF (414K)