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Structure paper

TitleAsymmetric pendrin homodimer reveals its molecular mechanism as anion exchanger.
Journal, issue, pagesNat Commun, Vol. 14, Issue 1, Page 3012, Year 2023
Publish dateMay 25, 2023
AuthorsQianying Liu / Xiang Zhang / Hui Huang / Yuxin Chen / Fang Wang / Aihua Hao / Wuqiang Zhan / Qiyu Mao / Yuxia Hu / Lin Han / Yifang Sun / Meng Zhang / Zhimin Liu / Geng-Lin Li / Weijia Zhang / Yilai Shu / Lei Sun / Zhenguo Chen /
PubMed AbstractPendrin (SLC26A4) is an anion exchanger expressed in the apical membranes of selected epithelia. Pendrin ablation causes Pendred syndrome, a genetic disorder associated with sensorineural hearing ...Pendrin (SLC26A4) is an anion exchanger expressed in the apical membranes of selected epithelia. Pendrin ablation causes Pendred syndrome, a genetic disorder associated with sensorineural hearing loss, hypothyroid goiter, and reduced blood pressure. However its molecular structure has remained unknown, limiting our understanding of the structural basis of transport. Here, we determine the cryo-electron microscopy structures of mouse pendrin with symmetric and asymmetric homodimer conformations. The asymmetric homodimer consists of one inward-facing protomer and the other outward-facing protomer, representing coincident uptake and secretion- a unique state of pendrin as an electroneutral exchanger. The multiple conformations presented here provide an inverted alternate-access mechanism for anion exchange. The structural and functional data presented here disclose the properties of an anion exchange cleft and help understand the importance of disease-associated variants, which will shed light on the pendrin exchange mechanism.
External linksNat Commun / PubMed:37230976 / PubMed Central
MethodsEM (single particle)
Resolution3.25 - 4.1 Å
Structure data

32555

7wk1

EMDB-32555, PDB-7wk1:
Mouse Pendrin bound chloride in inward state
Method: EM (single particle) / Resolution: 3.25 Å

32561

7wk7

EMDB-32561, PDB-7wk7:
Mouse Pendrin bound bicarbonate in inward state
Method: EM (single particle) / Resolution: 3.49 Å

32574

7wl2

EMDB-32574: mouse Pendrin in bicarbonate and iodide buffer in inward state
PDB-7wl2: Mouse Pendrin in bicarbonate and iodide buffer in inward state
Method: EM (single particle) / Resolution: 3.25 Å

32576

7wl7

EMDB-32576, PDB-7wl7:
Mouse Pendrin in chloride and bicarbonate buffer in inward state
Method: EM (single particle) / Resolution: 3.51 Å

32577

7wl8

EMDB-32577, PDB-7wl8:
Mouse Pendrin in chloride and iodide buffer in inward state
Method: EM (single particle) / Resolution: 3.4 Å

32578

7wl9

EMDB-32578, PDB-7wl9:
Mouse Pendrin in chloride and bicarbonate in asymmetric state
Method: EM (single particle) / Resolution: 3.78 Å

32579

7wla

EMDB-32579, PDB-7wla:
Mouse Pendrin in bicarbonate and iodide buffer in asymmetric state
Method: EM (single particle) / Resolution: 3.76 Å

32580

7wlb

EMDB-32580, PDB-7wlb:
Mouse Pendrin in chloride and iodide buffer in asymmetric state
Method: EM (single particle) / Resolution: 4.1 Å

32583

7wle

EMDB-32583, PDB-7wle:
Mouse Pendrin in chloride and bicarbonate buffer in outward state
Method: EM (single particle) / Resolution: 3.62 Å

EMDB-33232: Local refinement of outward-open TM domain of mouse Pendrin in chloride and bicarbonate in asymmetric state
Method: EM (single particle) / Resolution: 3.7 Å

Chemicals

ChemComp-CL:
Unknown entry

ChemComp-BCT:
BICARBONATE ION / pH buffer*YM

Source
  • mus musculus (house mouse)
KeywordsTRANSPORT PROTEIN / exchange / transport / slc

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