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TitleStructure of the membrane domain of human erythrocyte anion exchanger 1 revealed by electron crystallography.
Journal, issue, pagesJ Mol Biol, Vol. 397, Issue 1, Page 179-189, Year 2010
Publish dateMar 19, 2010
AuthorsTomohiro Yamaguchi / Yohei Ikeda / Yoshito Abe / Hiroyuki Kuma / Dongchon Kang / Naotaka Hamasaki / Teruhisa Hirai /
PubMed AbstractThe membrane domain of human erythrocyte anion exchanger 1 (AE1) works as a Cl(-)/HCO(3)(-) antiporter. This exchange is a key step for CO(2)/O(2) circulation in the blood. In spite of their ...The membrane domain of human erythrocyte anion exchanger 1 (AE1) works as a Cl(-)/HCO(3)(-) antiporter. This exchange is a key step for CO(2)/O(2) 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-A 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.
External linksJ Mol Biol / PubMed:20100494
MethodsEM (electron crystallography)
Resolution7.5 Å
Structure data

EMDB-1645:
Structure of human erythrocyte anion exchanger 1 revealed by electron crystallography.
Method: EM (electron crystallography) / Resolution: 7.5 Å

Source
  • Homo sapiens (human)

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