9kc9

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m (Protected "9kc9" [edit=sysop:move=sysop])
Current revision (06:37, 19 March 2025) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 9kc9 is ON HOLD
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==Cryo-EM structure of docked mouse bestrophin-1 in a partial open state==
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<StructureSection load='9kc9' size='340' side='right'caption='[[9kc9]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[9kc9]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9KC9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9KC9 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.1&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9kc9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9kc9 OCA], [https://pdbe.org/9kc9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9kc9 RCSB], [https://www.ebi.ac.uk/pdbsum/9kc9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9kc9 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/BEST1_MOUSE BEST1_MOUSE] Ligand-gated anion channel that allows the movement of anions across cell membranes when activated by calcium (Ca2+) (By similarity). Allows the movement of chloride and hydrogencarbonate (By similarity). Found in a partially open conformation leading to significantly smaller chloride movement (By similarity). Upon F2R/PAR-1 activation, the sequestered calcium is released into the cytosol of astrocytes, leading to the (Ca2+)-dependent release of L-glutamate into the synaptic cleft that targets the neuronal postsynaptic GRIN2A/NMDAR receptor resulting in the synaptic plasticity regulation (PubMed:23021213, PubMed:25645137, PubMed:29121962). Upon activation of the norepinephrine-alpha-1 adrenergic receptor signaling pathway, transports as well D-serine than L-glutamate in a (Ca2+)-dependent manner, leading to activation of adjacent NMDAR receptors and therefore regulates the heterosynaptic long-term depression and metaplasticity during initial memory acquisition (PubMed:34952697). Releases the 4-aminobutanoate neurotransmitter in a (Ca2+)-dependent manner, and participates in its tonic release from cerebellar glial cells (PubMed:20929730).[UniProtKB:O76090]<ref>PMID:20929730</ref> <ref>PMID:23021213</ref> <ref>PMID:25645137</ref> <ref>PMID:29121962</ref> <ref>PMID:34952697</ref> [https://www.uniprot.org/uniprot/C562_ECOLX C562_ECOLX] Electron-transport protein of unknown function.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Bestrophin 1 (BEST1) channels are calcium-activated Cl(-) channels involved in diverse physiological processes, including gliotransmitter release in astrocytes. Although human and chicken BEST1 orthologs have been extensively studied, the structural and functional properties of mouse BEST1 (mBEST1) remain poorly understood. In this study, we characterized the structure-function of mBEST1-BF, a C-terminally tagged variant, using whole-cell patch-clamp recordings, surface biotinylation assays, and single-particle cryo-electron microscopy. Cryo-electron microscopy structural analysis of mBEST1-BF revealed closed and partially open conformations. Comparative analysis with human and chicken BEST1 orthologs highlighted conserved calcium-binding and gating mechanisms, with distinct features in mBEST1, including a wider aperture sufficient to accommodate dehydrated Cl(-) ions and potential anion-binding sites near Val205 and Gln208 residues. The disordered C-terminal region of mBEST1 remains unresolved, suggesting it may require stabilizing factors for structural determination. Additionally, the autoinhibitory domain, which includes Ser354, likely plays a key role in regulating gating, with Ser354 potentially serving as a phosphorylation site that modulates channel activity. Our findings provide structural and functional insights into mBEST1 and suggest mechanisms underlying its unique gating and ion permeation properties.
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Authors: Lim, H.H., Kim, K.W., Ko, A.
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Cryo-EM structures of mouse bestrophin 1 channel in closed and partially open conformations.,Kim KW, Lee E, Ko A, Hwang J, Park K, Lee BC, Kim KW, Oh WJ, Kim K, Lim HH Mol Cells. 2025 Mar 3;48(5):100208. doi: 10.1016/j.mocell.2025.100208. PMID:40043778<ref>PMID:40043778</ref>
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Description: Cryo-EM structure of docked mouse bestrophin-1 in a partial open state
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Kim, K.W]]
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<div class="pdbe-citations 9kc9" style="background-color:#fffaf0;"></div>
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[[Category: Ko, A]]
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== References ==
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[[Category: Lim, H.H]]
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Escherichia coli]]
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[[Category: Large Structures]]
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[[Category: Mus musculus]]
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[[Category: Kim KW]]
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[[Category: Ko A]]
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[[Category: Lim HH]]

Current revision

Cryo-EM structure of docked mouse bestrophin-1 in a partial open state

PDB ID 9kc9

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