Molluscan hemocyanin: structure, evolution, and physiology

Sanae Kato, Takashi Matsui, Christos Gatsogiannis, Yoshikazu Tanaka

Research output: Contribution to journalReview articlepeer-review

15 Citations (Scopus)

Abstract

Most molluscs have blue blood because their respiratory molecule is hemocyanin, a type-3 copper-binding protein that turns blue upon oxygen binding. Molluscan hemocyanins are huge cylindrical multimeric glycoproteins that are found freely dissolved in the hemolymph. With molecular masses ranging from 3.3 to 13.5 MDa, molluscan hemocyanins are among the largest known proteins. They form decamers or multi-decamers of 330- to 550-kDa subunits comprising more than seven paralogous functional units. Based on the organization of functional domains, they assemble to form decamers, di-decamers, and tri-decamers. Their structure has been investigated using a combination of single particle electron cryo-microsopy of the entire structure and high-resolution X-ray crystallography of the functional unit, although, the one exception is squid hemocyanin for which a crystal structure analysis of the entire molecule has been carried out. In this review, we explain the molecular characteristics of molluscan hemocyanin mainly from the structural viewpoint, in which the structure of the functional unit, architecture of the huge cylindrical multimer, relationship between the composition of the functional unit and entire tertiary structure, and possible functions of the carbohydrates are introduced. We also discuss the evolutionary implications and physiological significance of molluscan hemocyanin.

Original languageEnglish
Pages (from-to)191-202
Number of pages12
JournalBiophysical Reviews
Volume10
Issue number2
DOIs
Publication statusPublished - 2018 Apr 1

Keywords

  • Electron cryo-microscopy
  • Evolution
  • Glycoprotein
  • Molluscan hemocyanin
  • Oxygen transporter
  • Structure
  • X-ray crystallography

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Molecular Biology

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