Binding mode of azide to ferric Aplysia limacina myoglobin. Crystallographic analysis at 1.9 A resolution.

A. Mattevi, G. Gatti, A. Coda, M. Rizzi, P. Ascenzi, M. Brunori, M. Bolognesi

Research output: Contribution to journalArticle

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Abstract

The binding mode of azide to the ferric form of Aplysia limacina myoglobin has been studied by X-ray crystallography. The three-dimensional structure of the complex has been refined at 1.9 A resolution to a crystallographic R-factor of 13.9%, including 126 ordered solvent molecules. Azide binds to the heme iron, at the sixth co-ordination position, and is oriented towards the outer part of the distal site crevice. This orientation is stabilized by an ionic interaction with the side-chain of Arg66 (E10) which, from an outer orientation in the 'aquo-met' ligand-free myoglobin, folds back towards the distal site in the presence of the anionic ligand. In the absence of a hydrogen bond donor residue at the distal E7 position in Aplysia limacina myoglobin, a different polar residue, Arg66 at the E10 topological position, has been selected by molecular evolution in order to grant ligand stabilization.

Original languageEnglish
Pages (from-to)1-6
Number of pages6
JournalJournal of molecular recognition : JMR
Volume4
Issue number1
Publication statusPublished - Feb 1991

Fingerprint

Aplysia
Azides
Myoglobin
Ligands
R388
Molecular Evolution
X ray crystallography
X Ray Crystallography
Heme
Hydrogen
Hydrogen bonds
Iron
Stabilization
Molecules

ASJC Scopus subject areas

  • Biochemistry
  • Genetics
  • Molecular Biology
  • Computer Vision and Pattern Recognition
  • Immunology

Cite this

Mattevi, A., Gatti, G., Coda, A., Rizzi, M., Ascenzi, P., Brunori, M., & Bolognesi, M. (1991). Binding mode of azide to ferric Aplysia limacina myoglobin. Crystallographic analysis at 1.9 A resolution. Journal of molecular recognition : JMR, 4(1), 1-6.

Binding mode of azide to ferric Aplysia limacina myoglobin. Crystallographic analysis at 1.9 A resolution. / Mattevi, A.; Gatti, G.; Coda, A.; Rizzi, M.; Ascenzi, P.; Brunori, M.; Bolognesi, M.

In: Journal of molecular recognition : JMR, Vol. 4, No. 1, 02.1991, p. 1-6.

Research output: Contribution to journalArticle

Mattevi, A, Gatti, G, Coda, A, Rizzi, M, Ascenzi, P, Brunori, M & Bolognesi, M 1991, 'Binding mode of azide to ferric Aplysia limacina myoglobin. Crystallographic analysis at 1.9 A resolution.', Journal of molecular recognition : JMR, vol. 4, no. 1, pp. 1-6.
Mattevi, A. ; Gatti, G. ; Coda, A. ; Rizzi, M. ; Ascenzi, P. ; Brunori, M. ; Bolognesi, M. / Binding mode of azide to ferric Aplysia limacina myoglobin. Crystallographic analysis at 1.9 A resolution. In: Journal of molecular recognition : JMR. 1991 ; Vol. 4, No. 1. pp. 1-6.
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