8Y5Z
human NaS1 inward state
8Y5Z の概要
エントリーDOI | 10.2210/pdb8y5z/pdb |
EMDBエントリー | 38960 |
分子名称 | Solute carrier family 13 member 1, SULFATE ION, SODIUM ION (3 entities in total) |
機能のキーワード | membrane sodium anion transproter, protein transport |
由来する生物種 | Homo sapiens (human) |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 132607.82 |
構造登録者 | |
主引用文献 | Chen, X.,Zhang, Y.,Yin, J.,Liu, C.,Xie, M.,Wang, Y.,Chen, M.,Zhang, R.,Yuan, X.,Li, D.,Chen, X.,Gao, X.,Cai, G.,Zhang, S.,Zhou, B.,Yang, M. Structural basis for the reaction cycle and transport mechanism of human Na + -sulfate cotransporter NaS1 (SLC13A1). Sci Adv, 10:eado6778-eado6778, 2024 Cited by PubMed Abstract: Sulfate (SO) is a pivotal inorganic anion with essential roles in mammalian physiology. NaS1, a member of solute carrier 13 family and divalent anion/sodium symporter family, functions as a Na-sulfate cotransporter, facilitating sulfate (re)absorption across renal proximal tubule and small intestine epithelia. While previous studies have linked several human disorders to mutations in the gene, its transport mechanism remains unclear. Here, we report the cryo-electron microscopy structures of five distinct conformations of the human NaS1 at resolutions of 2.7 to 3.3 angstroms, revealing the substrates recognition mechanism and the conformational change of NaS1 during the Na-sulfate cotransport cycle. Our studies delineate the molecular basis of the detailed dynamic transport cycle of NaS1. These findings advance the current understanding of the Na-sulfate cotransport mechanism, human sulfate (re)absorption, and the implications of disease-associated NaS1 mutations. PubMed: 39576865DOI: 10.1126/sciadv.ado6778 主引用文献が同じPDBエントリー |
実験手法 | ELECTRON MICROSCOPY (3.35 Å) |
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