TY - JOUR
T1 - Structure of the Membrane Domain of Human Erythrocyte Anion Exchanger 1 Revealed by Electron Crystallography
AU - Yamaguchi, Tomohiro
AU - Ikeda, Yohei
AU - Abe, Yoshito
AU - Kuma, Hiroyuki
AU - Kang, Dongchon
AU - Hamasaki, Naotaka
AU - Hirai, Teruhisa
N1 - Funding Information:
This work was supported by the Japan New Energy and Industrial Technology Development Organization. We thank Ms. T. Ogata for technical assistance. We also thank Drs. Y. Hiroaki and Y. Fujiyoshi for help with electron microscopy.
PY - 2010/3/19
Y1 - 2010/3/19
N2 - The membrane domain of human erythrocyte anion exchanger 1 (AE1) works as a Cl-/HCO3- antiporter. This exchange is a key step for CO2/O2 circulation in the blood. In spite of their importance, structural information about AE1 and the AE (anion exchanger) family are still very limited. We used electron microscopy to solve the three-dimensional structure of the AE1 membrane domain, fixed in an outward-open conformation by cross-linking, at 7.5-Å resolution. A dimer of AE1 membrane domains packed in two-dimensional array showed a projection map similar to that of the prokaryotic homolog of the ClC chloride channel, a Cl-/H+ antiporter. In a three-dimensional map, there are V-shaped densities near the center of the dimer and slightly narrower V-shaped clusters at a greater distance from the center of the dimer. These appear to be inserted into the membrane from opposite sides. The structural motifs, two homologous pairs of helices in internal repeats of the ClC transporter (helices B + C and J + K), are well fitted to those AE1 densities after simple domain movement.
AB - The membrane domain of human erythrocyte anion exchanger 1 (AE1) works as a Cl-/HCO3- antiporter. This exchange is a key step for CO2/O2 circulation in the blood. In spite of their importance, structural information about AE1 and the AE (anion exchanger) family are still very limited. We used electron microscopy to solve the three-dimensional structure of the AE1 membrane domain, fixed in an outward-open conformation by cross-linking, at 7.5-Å resolution. A dimer of AE1 membrane domains packed in two-dimensional array showed a projection map similar to that of the prokaryotic homolog of the ClC chloride channel, a Cl-/H+ antiporter. In a three-dimensional map, there are V-shaped densities near the center of the dimer and slightly narrower V-shaped clusters at a greater distance from the center of the dimer. These appear to be inserted into the membrane from opposite sides. The structural motifs, two homologous pairs of helices in internal repeats of the ClC transporter (helices B + C and J + K), are well fitted to those AE1 densities after simple domain movement.
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U2 - 10.1016/j.jmb.2010.01.027
DO - 10.1016/j.jmb.2010.01.027
M3 - Article
C2 - 20100494
AN - SCOPUS:77249153631
SN - 0022-2836
VL - 397
SP - 179
EP - 189
JO - Journal of Molecular Biology
JF - Journal of Molecular Biology
IS - 1
ER -