抄録
The C-terminal membrane domain of erythrocyte band 3 functions as an anion exchanger. Here, we report the three-dimensional (3D) structure of the membrane domain in an inhibitor-stabilized, outward-open conformation at 18 Å resolution. Unstained, frozen-hydrated tubular crystals containing the membrane domain of band 3 purified from human red blood cells (hB3MD) were examined using cryo-electron microscopy and iterative helical real-space reconstruction (IHRSR). The 3D image reconstruction of the tubular crystals showed the molecular packing of hB3MD dimers with dimensions of 60 × 110 Å in the membrane plane and a thickness of 70 Å across the membrane. Immunoelectron microscopy and carboxyl-terminal digestion demonstrated that the intracellular surface of hB3MD was exposed on the outer surface of the tubular crystal. A 3D density map revealed that hB3MD consists of at least two subdomains and that the outward-open form is characterized by a large hollow area on the extracellular surface and continuous density on the intracellular surface.
| 元の言語 | 英語 |
|---|---|
| ページ（範囲） | 406-412 |
| ページ数 | 7 |
| ジャーナル | Journal of structural biology |
| 巻 | 169 |
| 発行部数 | 3 |
| DOI | |
| 出版物ステータス | 出版済み - 3 1 2010 |
Fingerprint
All Science Journal Classification (ASJC) codes
- Structural Biology
これを引用
Helical image reconstruction of the outward-open human erythrocyte band 3 membrane domain in tubular crystals. / Yamaguchi, Tomohiro; Fujii, Takashi; Abe, Yoshito; Hirai, Teruhisa; Kang, Dongchon; Namba, Keiichi; Hamasaki, Naotaka; Mitsuoka, Kaoru.
：: Journal of structural biology, 巻 169, 番号 3, 01.03.2010, p. 406-412.研究成果: ジャーナルへの寄稿 › 記事
}
TY - JOUR
T1 - Helical image reconstruction of the outward-open human erythrocyte band 3 membrane domain in tubular crystals
AU - Yamaguchi, Tomohiro
AU - Fujii, Takashi
AU - Abe, Yoshito
AU - Hirai, Teruhisa
AU - Kang, Dongchon
AU - Namba, Keiichi
AU - Hamasaki, Naotaka
AU - Mitsuoka, Kaoru
PY - 2010/3/1
Y1 - 2010/3/1
N2 - The C-terminal membrane domain of erythrocyte band 3 functions as an anion exchanger. Here, we report the three-dimensional (3D) structure of the membrane domain in an inhibitor-stabilized, outward-open conformation at 18 Å resolution. Unstained, frozen-hydrated tubular crystals containing the membrane domain of band 3 purified from human red blood cells (hB3MD) were examined using cryo-electron microscopy and iterative helical real-space reconstruction (IHRSR). The 3D image reconstruction of the tubular crystals showed the molecular packing of hB3MD dimers with dimensions of 60 × 110 Å in the membrane plane and a thickness of 70 Å across the membrane. Immunoelectron microscopy and carboxyl-terminal digestion demonstrated that the intracellular surface of hB3MD was exposed on the outer surface of the tubular crystal. A 3D density map revealed that hB3MD consists of at least two subdomains and that the outward-open form is characterized by a large hollow area on the extracellular surface and continuous density on the intracellular surface.
AB - The C-terminal membrane domain of erythrocyte band 3 functions as an anion exchanger. Here, we report the three-dimensional (3D) structure of the membrane domain in an inhibitor-stabilized, outward-open conformation at 18 Å resolution. Unstained, frozen-hydrated tubular crystals containing the membrane domain of band 3 purified from human red blood cells (hB3MD) were examined using cryo-electron microscopy and iterative helical real-space reconstruction (IHRSR). The 3D image reconstruction of the tubular crystals showed the molecular packing of hB3MD dimers with dimensions of 60 × 110 Å in the membrane plane and a thickness of 70 Å across the membrane. Immunoelectron microscopy and carboxyl-terminal digestion demonstrated that the intracellular surface of hB3MD was exposed on the outer surface of the tubular crystal. A 3D density map revealed that hB3MD consists of at least two subdomains and that the outward-open form is characterized by a large hollow area on the extracellular surface and continuous density on the intracellular surface.
UR - http://www.scopus.com/inward/record.url?scp=76749162402&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=76749162402&partnerID=8YFLogxK
U2 - 10.1016/j.jsb.2009.12.009
DO - 10.1016/j.jsb.2009.12.009
M3 - Article
C2 - 20005958
AN - SCOPUS:76749162402
VL - 169
SP - 406
EP - 412
JO - Journal of Structural Biology
JF - Journal of Structural Biology
SN - 1047-8477
IS - 3
ER -