Crystal Structure of the 3.8-MDa Respiratory Supermolecule Hemocyanin at 3.0 Å Resolution

Zuoqi Gai, Asuka Matsuno, Koji Kato, Sanae Kato, Md Rafiqul Islam Khan, Takeshi Shimizu, Takeya Yoshioka, Yuki Kato, Hideki Kishimura, Gaku Kanno, Yoshikatsu Miyabe, Tohru Terada, Yoshikazu Tanaka, Min Yao

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

Summary Molluscan hemocyanin, a copper-containing oxygen transporter, is one of the largest known proteins. Although molluscan hemocyanins are currently applied as immunotherapeutic agents, their precise structure has not been determined because of their enormous size. Here, we have determined the first X-ray crystal structure of intact molluscan hemocyanin. The structure unveiled the architecture of the 3.8-MDa supermolecule composed of homologous functional units (FUs), wherein the dimers of FUs hierarchically associated to form the entire cylindrical decamer. Most of the specific inter-FU interactions were localized at narrow regions in the FU dimers, suggesting that rigid FU dimers formed by specific interactions assemble with flexibility. Furthermore, the roles of carbohydrates in assembly and allosteric effect, and conserved sulfur-containing residues in copper incorporation, were revealed. The precise structural information obtained in this study will accelerate our understanding of the molecular basis of hemocyanin and its future applications.

Original languageEnglish
Pages (from-to)2204-2212
Number of pages9
JournalStructure
Volume23
Issue number12
DOIs
Publication statusPublished - Dec 1 2015
Externally publishedYes

Fingerprint

Hemocyanin
Copper
Sulfur
Carbohydrates
X-Rays
Oxygen
Proteins

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

Cite this

Gai, Z., Matsuno, A., Kato, K., Kato, S., Khan, M. R. I., Shimizu, T., ... Yao, M. (2015). Crystal Structure of the 3.8-MDa Respiratory Supermolecule Hemocyanin at 3.0 Å Resolution. Structure, 23(12), 2204-2212. https://doi.org/10.1016/j.str.2015.09.008

Crystal Structure of the 3.8-MDa Respiratory Supermolecule Hemocyanin at 3.0 Å Resolution. / Gai, Zuoqi; Matsuno, Asuka; Kato, Koji; Kato, Sanae; Khan, Md Rafiqul Islam; Shimizu, Takeshi; Yoshioka, Takeya; Kato, Yuki; Kishimura, Hideki; Kanno, Gaku; Miyabe, Yoshikatsu; Terada, Tohru; Tanaka, Yoshikazu; Yao, Min.

In: Structure, Vol. 23, No. 12, 01.12.2015, p. 2204-2212.

Research output: Contribution to journalArticle

Gai, Z, Matsuno, A, Kato, K, Kato, S, Khan, MRI, Shimizu, T, Yoshioka, T, Kato, Y, Kishimura, H, Kanno, G, Miyabe, Y, Terada, T, Tanaka, Y & Yao, M 2015, 'Crystal Structure of the 3.8-MDa Respiratory Supermolecule Hemocyanin at 3.0 Å Resolution', Structure, vol. 23, no. 12, pp. 2204-2212. https://doi.org/10.1016/j.str.2015.09.008
Gai, Zuoqi ; Matsuno, Asuka ; Kato, Koji ; Kato, Sanae ; Khan, Md Rafiqul Islam ; Shimizu, Takeshi ; Yoshioka, Takeya ; Kato, Yuki ; Kishimura, Hideki ; Kanno, Gaku ; Miyabe, Yoshikatsu ; Terada, Tohru ; Tanaka, Yoshikazu ; Yao, Min. / Crystal Structure of the 3.8-MDa Respiratory Supermolecule Hemocyanin at 3.0 Å Resolution. In: Structure. 2015 ; Vol. 23, No. 12. pp. 2204-2212.
@article{4ee18b0df9af49adb42430cd1b318d74,
title = "Crystal Structure of the 3.8-MDa Respiratory Supermolecule Hemocyanin at 3.0 {\AA} Resolution",
abstract = "Summary Molluscan hemocyanin, a copper-containing oxygen transporter, is one of the largest known proteins. Although molluscan hemocyanins are currently applied as immunotherapeutic agents, their precise structure has not been determined because of their enormous size. Here, we have determined the first X-ray crystal structure of intact molluscan hemocyanin. The structure unveiled the architecture of the 3.8-MDa supermolecule composed of homologous functional units (FUs), wherein the dimers of FUs hierarchically associated to form the entire cylindrical decamer. Most of the specific inter-FU interactions were localized at narrow regions in the FU dimers, suggesting that rigid FU dimers formed by specific interactions assemble with flexibility. Furthermore, the roles of carbohydrates in assembly and allosteric effect, and conserved sulfur-containing residues in copper incorporation, were revealed. The precise structural information obtained in this study will accelerate our understanding of the molecular basis of hemocyanin and its future applications.",
author = "Zuoqi Gai and Asuka Matsuno and Koji Kato and Sanae Kato and Khan, {Md Rafiqul Islam} and Takeshi Shimizu and Takeya Yoshioka and Yuki Kato and Hideki Kishimura and Gaku Kanno and Yoshikatsu Miyabe and Tohru Terada and Yoshikazu Tanaka and Min Yao",
year = "2015",
month = "12",
day = "1",
doi = "10.1016/j.str.2015.09.008",
language = "English",
volume = "23",
pages = "2204--2212",
journal = "Structure with Folding & design",
issn = "0969-2126",
publisher = "Cell Press",
number = "12",

}

TY - JOUR

T1 - Crystal Structure of the 3.8-MDa Respiratory Supermolecule Hemocyanin at 3.0 Å Resolution

AU - Gai, Zuoqi

AU - Matsuno, Asuka

AU - Kato, Koji

AU - Kato, Sanae

AU - Khan, Md Rafiqul Islam

AU - Shimizu, Takeshi

AU - Yoshioka, Takeya

AU - Kato, Yuki

AU - Kishimura, Hideki

AU - Kanno, Gaku

AU - Miyabe, Yoshikatsu

AU - Terada, Tohru

AU - Tanaka, Yoshikazu

AU - Yao, Min

PY - 2015/12/1

Y1 - 2015/12/1

N2 - Summary Molluscan hemocyanin, a copper-containing oxygen transporter, is one of the largest known proteins. Although molluscan hemocyanins are currently applied as immunotherapeutic agents, their precise structure has not been determined because of their enormous size. Here, we have determined the first X-ray crystal structure of intact molluscan hemocyanin. The structure unveiled the architecture of the 3.8-MDa supermolecule composed of homologous functional units (FUs), wherein the dimers of FUs hierarchically associated to form the entire cylindrical decamer. Most of the specific inter-FU interactions were localized at narrow regions in the FU dimers, suggesting that rigid FU dimers formed by specific interactions assemble with flexibility. Furthermore, the roles of carbohydrates in assembly and allosteric effect, and conserved sulfur-containing residues in copper incorporation, were revealed. The precise structural information obtained in this study will accelerate our understanding of the molecular basis of hemocyanin and its future applications.

AB - Summary Molluscan hemocyanin, a copper-containing oxygen transporter, is one of the largest known proteins. Although molluscan hemocyanins are currently applied as immunotherapeutic agents, their precise structure has not been determined because of their enormous size. Here, we have determined the first X-ray crystal structure of intact molluscan hemocyanin. The structure unveiled the architecture of the 3.8-MDa supermolecule composed of homologous functional units (FUs), wherein the dimers of FUs hierarchically associated to form the entire cylindrical decamer. Most of the specific inter-FU interactions were localized at narrow regions in the FU dimers, suggesting that rigid FU dimers formed by specific interactions assemble with flexibility. Furthermore, the roles of carbohydrates in assembly and allosteric effect, and conserved sulfur-containing residues in copper incorporation, were revealed. The precise structural information obtained in this study will accelerate our understanding of the molecular basis of hemocyanin and its future applications.

UR - http://www.scopus.com/inward/record.url?scp=84949203424&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84949203424&partnerID=8YFLogxK

U2 - 10.1016/j.str.2015.09.008

DO - 10.1016/j.str.2015.09.008

M3 - Article

C2 - 26602184

AN - SCOPUS:84949203424

VL - 23

SP - 2204

EP - 2212

JO - Structure with Folding & design

JF - Structure with Folding & design

SN - 0969-2126

IS - 12

ER -