4YZF

Crystal structure of the anion exchanger domain of human erythrocyte Band 3

Summary for 4YZF

• Entry DOI: 10.2210/pdb4yzf/pdb
• Descriptor: Band 3 anion transport protein, FAB fragment of Immunoglobulin (IgG) molecule, 2,2'-ethane-1,2-diylbis{5-[(sulfanylmethyl)amino]benzenesulfonic acid}, ... (4 entities in total)
• Functional Keywords: immune system, human membrane protein, anion exchanger, erythrocytes
• Biological source: Homo sapiens (Human); More
• Cellular location: Cell membrane ; Multi-pass membrane protein: P02730
• Total number of polymer chains: 12
• Total formula weight: 601715.14

Authors

Alguel, Y.,Arakawa, T.,Yugiri, T.K.,Iwanari, H.,Hatae, H.,Iwata, M.,Abe, Y.,Hino, T.,Suno, C.I.,Kuma, H.,Kang, D.,Murata, T.,Hamakubo, T.,Cameron, A.D.,Kobayashi, T.,Hamasaki, N.,Iwata, S. (deposition date: 2015-03-25, release date: 2015-11-04, Last modification date: 2024-10-16)

Primary citation

Arakawa, T.,Kobayashi-Yurugi, T.,Alguel, Y.,Iwanari, H.,Hatae, H.,Iwata, M.,Abe, Y.,Hino, T.,Ikeda-Suno, C.,Kuma, H.,Kang, D.,Murata, T.,Hamakubo, T.,Cameron, A.D.,Kobayashi, T.,Hamasaki, N.,Iwata, S.
Crystal structure of the anion exchanger domain of human erythrocyte band 3.
Science, 350:680-684, 2015

PubMed Abstract: Anion exchanger 1 (AE1), also known as band 3 or SLC4A1, plays a key role in the removal of carbon dioxide from tissues by facilitating the exchange of chloride and bicarbonate across the plasma membrane of erythrocytes. An isoform of AE1 is also present in the kidney. Specific mutations in human AE1 cause several types of hereditary hemolytic anemias and/or distal renal tubular acidosis. Here we report the crystal structure of the band 3 anion exchanger domain (AE1(CTD)) at 3.5 angstroms. The structure is locked in an outward-facing open conformation by an inhibitor. Comparing this structure with a substrate-bound structure of the uracil transporter UraA in an inward-facing conformation allowed us to identify the anion-binding position in the AE1(CTD), and to propose a possible transport mechanism that could explain why selected mutations lead to disease.

PubMed: 26542571
DOI: 10.1126/science.aaa4335

Experimental method

X-RAY DIFFRACTION (3.5 Å)