Journal
JOURNAL OF STRUCTURAL BIOLOGY
Volume 169, Issue 3, Pages 406-412Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.jsb.2009.12.009
Keywords
Band 3; Membrane protein structure; Cryo-electron microscopy; Tubular crystal; Iterative helical real-space reconstruction
Funding
- Ministry of Education, Culture, Sports, Science, and Technology of Japan [16087207]
- Japan New Energy and Industrial Technology Development Organization (NEDO)
- Grants-in-Aid for Scientific Research [20370065, 16087207] Funding Source: KAKEN
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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 angstrom 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 x 110 angstrom in the membrane plane and a thickness of 70 A 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. (C) 2009 Elsevier Inc. All rights reserved
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