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Structure paper

TitleStructural insights into the mechanisms of urea permeation and distinct inhibition modes of urea transporters.
Journal, issue, pagesNat Commun, Vol. 15, Issue 1, Page 10226, Year 2024
Publish dateNov 26, 2024
AuthorsShen-Ming Huang / Zhi-Zhen Huang / Lei Liu / Meng-Yao Xiong / Chao Zhang / Bo-Yang Cai / Ming-Wei Wang / Kui Cai / Ying-Li Jia / Jia-Le Wang / Ming-Hui Zhang / Yi-He Xie / Min Li / Hang Zhang / Cheng-Hao Weng / Xin Wen / Zhi Li / Ying Sun / Fan Yi / Zhao Yang / Peng Xiao / Fan Yang / Xiao Yu / Lu Tie / Bao-Xue Yang / Jin-Peng Sun /
PubMed AbstractUrea's transmembrane transport through urea transporters (UT) is a fundamental physiological behavior for life activities. Here, we present 11 cryo-EM structures of four UT members in resting states, ...Urea's transmembrane transport through urea transporters (UT) is a fundamental physiological behavior for life activities. Here, we present 11 cryo-EM structures of four UT members in resting states, urea transport states, or inactive states bound with synthetic competitive, uncompetitive or noncompetitive inhibitor. Our results indicate that the binding of urea via a conserved urea recognition motif (URM) and the urea transport via H-bond transfer along the Q-T-T-Q motif among different UT members. Moreover, distinct binding modes of the competitive inhibitors 25a and ATB3, the uncompetitive inhibitor CF11 and the noncompetitive inhibitor HQA2 provide different mechanisms for blocking urea transport and achieved selectivity through L-P pocket, UCBP region and SCG pocket, respectively. In summary, our study not only allows structural understanding of urea transport via UTs but also afforded a structural landscape of hUT-A2 inhibition by competitive, uncompetitive and noncompetitive inhibitors, which may facilitate developing selective human UT-A inhibitors as a new class of salt-sparing diuretics.
External linksNat Commun / PubMed:39587082 / PubMed Central
MethodsEM (single particle)
Resolution2.3 - 3.3 Å
Structure data

38268

8xd7

EMDB-38268, PDB-8xd7:
Cryo-EM structure of inhibitor 25a bound human urea transporter A2.
Method: EM (single particle) / Resolution: 2.6 Å

38270

8xd9

EMDB-38270, PDB-8xd9:
Cryo-EM structure of human urea transporter A2.
Method: EM (single particle) / Resolution: 2.8 Å

38271

8xda

EMDB-38271, PDB-8xda:
Cryo-EM structure of urea bound human urea transporter A2.
Method: EM (single particle) / Resolution: 3.0 Å

38272

8xdb

EMDB-38272, PDB-8xdb:
Cryo-EM structure of human urea transporter A2.
Method: EM (single particle) / Resolution: 3.3 Å

38273

8xdc

EMDB-38273, PDB-8xdc:
Cryo-EM structure of human urea transporter A2.
Method: EM (single particle) / Resolution: 3.0 Å

38274

8xdd

EMDB-38274, PDB-8xdd:
Cryo-EM structure of human urea transporter A2.
Method: EM (single particle) / Resolution: 3.0 Å

38275

8xde

EMDB-38275, PDB-8xde:
Cryo-EM structure of human urea transporter A3.
Method: EM (single particle) / Resolution: 2.3 Å

38276

8xdf

EMDB-38276, PDB-8xdf:
Cryo-EM structure of human urea transporter B.
Method: EM (single particle) / Resolution: 2.4 Å

38277

8xdg

EMDB-38277, PDB-8xdg:
Cryo-EM structure of zebrafish urea transporter.
Method: EM (single particle) / Resolution: 3.1 Å

38278

8xdh

EMDB-38278, PDB-8xdh:
Cryo-EM structure of zebrafish urea transporter.
Method: EM (single particle) / Resolution: 3.1 Å

38279

8xdi

EMDB-38279, PDB-8xdi:
Cryo-EM structure of zebrafish urea transporter.
Method: EM (single particle) / Resolution: 3.1 Å

Chemicals

PDB-1lu9:
Structure of methylene-tetrahydromethanopterin dehydrogenase from Methylobacterium extorquens AM1

ChemComp-URE:
UREA

ChemComp-HOH:
WATER

PDB-1lyj:
DISSECTION OF HELIX CAPPING IN T4 LYSOZYME BY STRUCTURAL AND THERMODYNAMIC ANALYSIS OF SIX AMINO ACID SUBSTITUTIONS AT THR 59

PDB-1lva:
Crystal structure of a C-terminal fragment of Moorella thermoacetica elongation factor SelB

ChemComp-8HC:
8-hydroxyquinoline-2-carboxylic acid

ChemComp-SZ4:
1-(3-methoxyphenyl)methanamine

Source
  • homo sapiens (human)
  • homo sapien (human)
  • danio rerio (zebrafish)
KeywordsMEMBRANE PROTEIN / Urea transporter

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