超巨大タンパク質会合体ヘモシアニンのX線結晶構造解析

  • 松野 明日香
    北海道大学大学院生命科学院
  • 田中 良和
    北海道大学大学院先端生命科学研究院 独立行政法人科学技術振興機構 さきがけ

書誌事項

タイトル別名
  • Crystal Structure Analysis of a Huge Oxygen Transport Supermolecule Hemocyanin
  • チョウキョダイ タンパクシツ カイゴウタイ ヘモシアニン ノ Xセン ケッショウ コウゾウ カイセキ

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抄録

Many molluscs use hemocyanin freely dissolved in hemolymph for oxygen transportation. Hemocyanin is one of the largest known proteins, of which total molecular mass is larger than 3.3 MDa. Although molluscan hemocyanin is used as immunotherapeutic agents, their detailed structures had not yet been revealed. As its enormous size and the propensity of dissociation hampered crystallization, structural studies have relied mainly on electron microscopy. To understand the oxygen transportation mechanism in detail and promote the biomedical application, high-resolution structure has been desired for a long time. In this study, we successfully determined the X-ray crystal structure of the intact 3.8-MDa hemocyanin from Japanese flying squid at 3.0 Å resolution, which revealed the detailed molecular architecture of the supermolecule.

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