7wlb

From Proteopedia

(Difference between revisions)

Revision as of 08:15, 16 August 2023

Mouse Pendrin in chloride and iodide buffer in asymmetric state

Structural highlights

7wlb is a 2 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 4.1Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

S26A4_MOUSE Sodium-independent transporter of chloride and iodide (By similarity). Mediates electroneutral iodide-chloride, iodide-bicarbonate and chloride-bicarbonate exchange with 1:1 stoichiometry (PubMed:11274445, PubMed:18565999). Mediates elctroneutral chloride-formate exchange (By similarity).[UniProtKB:Q9R154]^[1] ^[2]

Publication Abstract from PubMed

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.

Asymmetric pendrin homodimer reveals its molecular mechanism as anion exchanger.,Liu Q, Zhang X, Huang H, Chen Y, Wang F, Hao A, Zhan W, Mao Q, Hu Y, Han L, Sun Y, Zhang M, Liu Z, Li GL, Zhang W, Shu Y, Sun L, Chen Z Nat Commun. 2023 May 25;14(1):3012. doi: 10.1038/s41467-023-38303-0. PMID:37230976^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Royaux IE, Wall SM, Karniski LP, Everett LA, Suzuki K, Knepper MA, Green ED. Pendrin, encoded by the Pendred syndrome gene, resides in the apical region of renal intercalated cells and mediates bicarbonate secretion. Proc Natl Acad Sci U S A. 2001 Mar 27;98(7):4221-6. PMID:11274445 doi:10.1073/pnas.071516798
↑ Shcheynikov N, Yang D, Wang Y, Zeng W, Karniski LP, So I, Wall SM, Muallem S. The Slc26a4 transporter functions as an electroneutral Cl-/I-/HCO3 J Physiol. 2008 Aug 15;586(16):3813-24. PMID:18565999 doi:10.1113/jphysiol.2008.154468
↑ Liu Q, Zhang X, Huang H, Chen Y, Wang F, Hao A, Zhan W, Mao Q, Hu Y, Han L, Sun Y, Zhang M, Liu Z, Li GL, Zhang W, Shu Y, Sun L, Chen Z. Asymmetric pendrin homodimer reveals its molecular mechanism as anion exchanger. Nat Commun. 2023 May 25;14(1):3012. PMID:37230976 doi:10.1038/s41467-023-38303-0

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/7wlb"

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 7wlb is ON HOLD  until 2024-04-13
+==Mouse Pendrin in chloride and iodide buffer in asymmetric state==
+<StructureSection load='7wlb' size='340' side='right'caption='[[7wlb]], [[Resolution|resolution]] 4.10&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[7wlb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7WLB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7WLB FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.1&#8491;</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7wlb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7wlb OCA], [https://pdbe.org/7wlb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7wlb RCSB], [https://www.ebi.ac.uk/pdbsum/7wlb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7wlb ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/S26A4_MOUSE S26A4_MOUSE] Sodium-independent transporter of chloride and iodide (By similarity). Mediates electroneutral iodide-chloride, iodide-bicarbonate and chloride-bicarbonate exchange with 1:1 stoichiometry (PubMed:11274445, PubMed:18565999). Mediates elctroneutral chloride-formate exchange (By similarity).[UniProtKB:Q9R154]<ref>PMID:11274445</ref> <ref>PMID:18565999</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-Authors: Liu, Q.Y., Zhang, X., Sun, L., Chen, Z.G.
+Asymmetric pendrin homodimer reveals its molecular mechanism as anion exchanger.,Liu Q, Zhang X, Huang H, Chen Y, Wang F, Hao A, Zhan W, Mao Q, Hu Y, Han L, Sun Y, Zhang M, Liu Z, Li GL, Zhang W, Shu Y, Sun L, Chen Z Nat Commun. 2023 May 25;14(1):3012. doi: 10.1038/s41467-023-38303-0. PMID:37230976<ref>PMID:37230976</ref>
-Description: Mouse Pendrin in chloride and iodide buffer in asymmetric state
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Chen, Z.G]]
+<div class="pdbe-citations 7wlb" style="background-color:#fffaf0;"></div>
-[[Category: Zhang, X]]
+== References ==
-[[Category: Liu, Q.Y]]
+<references/>
-[[Category: Sun, L]]
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Mus musculus]]
+[[Category: Chen ZG]]
+[[Category: Liu QY]]
+[[Category: Sun L]]
+[[Category: Zhang X]]

7wlb

From Proteopedia

Revision as of 08:15, 16 August 2023

Mouse Pendrin in chloride and iodide buffer in asymmetric state

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox