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TitleStructural basis for the transport and substrate selection of human urate transporter 1.
Journal, issue, pagesCell Rep, Vol. 43, Issue 8, Page 114628, Year 2024
Publish dateAug 27, 2024
AuthorsJingjing He / Guoyun Liu / Fang Kong / Qiulong Tan / Zhenzhou Wang / Meng Yang / Yonglin He / Xiaoxiao Jia / Chuangye Yan / Chao Wang / Hongwu Qian /
PubMed AbstractHigh serum urate levels are the major risk factor for gout. URAT1, the primary transporter for urate absorption in the kidneys, is well known as an anti-hyperuricemia drug target. However, the ...High serum urate levels are the major risk factor for gout. URAT1, the primary transporter for urate absorption in the kidneys, is well known as an anti-hyperuricemia drug target. However, the clinical application of URAT1-targeted drugs is limited because of their low specificity and severe side effects. The lack of structural information impedes elucidation of the transport mechanism and the development of new drugs. Here, we present the cryoelectron microscopy (cryo-EM) structures of human URAT1(R477S), its complex with urate, and its closely related homolog OAT4. URAT1(R477S) and OAT4 exhibit major facilitator superfamily (MFS) folds with outward- and inward-open conformations, respectively. Structural comparison reveals a 30° rotation between the N-terminal and C-terminal domains, supporting an alternating access mechanism. A conserved arginine (OAT4-Arg473/URAT1-Arg477) is found to be essential for chloride-mediated inhibition. The URAT1(R477S)-urate complex reveals the specificity of urate recognition. Taken together, our study promotes our understanding of the transport mechanism and substrate selection of URAT1.
External linksCell Rep / PubMed:39146184
MethodsEM (single particle)
Resolution3.0 - 3.8 Å
Structure data

37579

8wjg

EMDB-37579, PDB-8wjg:
Cryo-EM structure of URAT1(R477S)
Method: EM (single particle) / Resolution: 3.0 Å

37580

8wjh

EMDB-37580, PDB-8wjh:
Cryo-EM structure of OAT4
Method: EM (single particle) / Resolution: 3.1 Å

37589

8wjq

EMDB-37589, PDB-8wjq:
Cryo-EM structure of URAT1(R477S)-Urate complex
Method: EM (single particle) / Resolution: 3.8 Å

Chemicals

ChemComp-CL:
Unknown entry

ChemComp-URC:
URIC ACID

Source
  • homo sapiens (human)
KeywordsTRANSPORT PROTEIN / SLC

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