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| | <StructureSection load='4y7k' size='340' side='right'caption='[[4y7k]], [[Resolution|resolution]] 3.50Å' scene=''> | | <StructureSection load='4y7k' size='340' side='right'caption='[[4y7k]], [[Resolution|resolution]] 3.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4y7k]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Metac Metac]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Y7K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Y7K FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4y7k]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii_DSM_2661 Methanocaldococcus jannaschii DSM 2661] and [https://en.wikipedia.org/wiki/Methanosarcina_acetivorans_C2A Methanosarcina acetivorans C2A]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Y7K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Y7K FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4y7j|4y7j]]</td></tr> | + | </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=4y7k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y7k OCA], [https://pdbe.org/4y7k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4y7k RCSB], [https://www.ebi.ac.uk/pdbsum/4y7k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4y7k ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ribC, MJ1184 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=188937 METAC])</td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4y7k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y7k OCA], [http://pdbe.org/4y7k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4y7k RCSB], [http://www.ebi.ac.uk/pdbsum/4y7k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4y7k ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q8TNK0_METAC Q8TNK0_METAC] [https://www.uniprot.org/uniprot/RISC_METJA RISC_METJA] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Ion channels|Ion channels]] | + | *[[Ion channels 3D structures|Ion channels 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Metac]] | + | [[Category: Methanocaldococcus jannaschii DSM 2661]] |
| - | [[Category: Li, J]] | + | [[Category: Methanosarcina acetivorans C2A]] |
| - | [[Category: Liu, Z]] | + | [[Category: Li J]] |
| - | [[Category: Mechanosensation]] | + | [[Category: Liu Z]] |
| - | [[Category: Mechanosensitive channel]]
| + | |
| - | [[Category: Membrane protein]]
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| - | [[Category: Transport protein]]
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| Structural highlights
Function
Q8TNK0_METAC RISC_METJA
Publication Abstract from PubMed
The prokaryotic mechanosensitive channel of large conductance (MscL) is a pressure-relief valve protecting the cell from lysing during acute osmotic downshock. When the membrane is stretched, MscL responds to the increase of membrane tension and opens a nonselective pore to about 30 A wide, exhibiting a large unitary conductance of approximately 3 nS. A fundamental step toward understanding the gating mechanism of MscL is to decipher the molecular details of the conformational changes accompanying channel opening. By applying fusion-protein strategy and controlling detergent composition, we have solved the structures of an archaeal MscL homolog from Methanosarcina acetivorans trapped in the closed and expanded intermediate states. The comparative analysis of these two new structures reveals significant conformational rearrangements in the different domains of MscL. The large changes observed in the tilt angles of the two transmembrane helices (TM1 and TM2) fit well with the helix-pivoting model derived from the earlier geometric analyses based on the previous structures. Meanwhile, the periplasmic loop region transforms from a folded structure, containing an omega-shaped loop and a short beta-hairpin, to an extended and partly disordered conformation during channel expansion. Moreover, a significant rotating and sliding of the N-terminal helix (N-helix) is coupled to the tilting movements of TM1 and TM2. The dynamic relationships between the N-helix and TM1/TM2 suggest that the N-helix serves as a membrane-anchored stopper that limits the tilts of TM1 and TM2 in the gating process. These results provide direct mechanistic insights into the highly coordinated movement of the different domains of the MscL channel when it expands.
Mechanical coupling of the multiple structural elements of the large-conductance mechanosensitive channel during expansion.,Li J, Guo J, Ou X, Zhang M, Li Y, Liu Z Proc Natl Acad Sci U S A. 2015 Aug 10. pii: 201503202. PMID:26261325[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Li J, Guo J, Ou X, Zhang M, Li Y, Liu Z. Mechanical coupling of the multiple structural elements of the large-conductance mechanosensitive channel during expansion. Proc Natl Acad Sci U S A. 2015 Aug 10. pii: 201503202. PMID:26261325 doi:http://dx.doi.org/10.1073/pnas.1503202112
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