Research Article

Hexamers of subunit II from Limulus hemocyanin (a 48-mer) have the same quaternary structure as whole Panulirus hemocyanin molecules

  1. Karen A. Magnus1,†,
  2. Eaton E. Lattman1,*,
  3. Anne Volbeda2,‡,
  4. Wim G. J. Hol2

Article first published online: 3 FEB 2004

DOI: 10.1002/prot.340090403

Issue

Proteins: Structure, Function, and Bioinformatics

Proteins: Structure, Function, and Bioinformatics

Volume 9, Issue 4, pages 240–247, April 1991

Additional Information

How to Cite

Magnus, K. A., Lattman, E. E., Volbeda, A. and Hol, W. G. J. (1991), Hexamers of subunit II from Limulus hemocyanin (a 48-mer) have the same quaternary structure as whole Panulirus hemocyanin molecules. Proteins: Structure, Function, and Bioinformatics, 9: 240–247. doi: 10.1002/prot.340090403

Author Information

  1. 1

    Department of Biophysics, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205

  2. 2

    BIOSN Research Institute, University of Groningen, Nijenborgh 16, 9747 AG Groningen, The Netherlands

  1. †

    Department of Biochemistry, Case Western Reserve University, School of Medicine, Cleveland, OH 44106

  2. ‡

    Division of Biological Structures, European Molecular Biology Laboratory, Meyerhofstrasse, D-6900 Heidelberg, West Germany

*Department of Biophysics, Johns Hopkins Unversity School of Medicine, 725 N. Wolfe Street, Room 260, Wood Basic Science Building, Baltimore, MD 21205

Publication History

  1. Issue published online: 3 FEB 2004
  2. Article first published online: 3 FEB 2004
  3. Manuscript Revised: 2 OCT 1990
  4. Manuscript Received: 2 OCT 1989

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Keywords:

  • hemocyanin;
  • Limulus;
  • Panulirus;
  • horseshoe crab;
  • spiny lobster;
  • molecular replacement;
  • X-ray;
  • crystallography;
  • protein structure

Abstract

Hemocyanins are copper-containing proteins that transport oxygen in a variety of invertebrates. Considerable evidence has accumulated that arthropodan hemocyanins are multimers of a fundamental hexameric unit. X-Ray crystallographic structure determination has revealed that the hemocyanin molecule from the spiny lobster Panulirus interruptus is a single hexamer having 32 point group symmetry. Using crystals of subunit II, one of 8 polypeptide types comprising the octahexameric hemocyanin of the horseshoe crab Limulus polyphemus, and the molecular replacement method for crystallographic phase determination we show that subunit II forms assemblies with the same hexameric quaternary structure as the whole Panulirus hemocyanin molecule. Observation of the same hexameric motif in two widely separated species provides strong additional evidence that this quaternary structural unit is a universal building block of arthropodan hemocyanins.

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