6ctd | pdb_00006ctd

C-terminal domain truncation of the Mycobacterium tuberculosis Mechanosensitive Channel of Large Conductance MscL

spinqualitylabelsall models 6ctd, resolution 5.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6ctd is a 10 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: AU Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [MSCL_MYCTA] Channel that opens in response to stretch forces in the membrane lipid bilayer. The force required to trigger channel opening depends on the nature of the membrane lipids; the presence of phosphatidylinositol enhances mechanosensitivity of the channel. May participate in the regulation of osmotic pressure changes within the cell.[UniProtKB:P9WJN5] Publication Abstract from PubMed Microbial survival in dynamic environments requires the ability to successfully respond to abrupt changes in osmolarity. The mechanosensitive channel of large conductance (MscL) is a ubiquitous channel that facilitates the survival of bacteria and archaea under severe osmotic downshock conditions by relieving excess turgor pressure in response to increased membrane tension. A prominent structural feature of MscL, the cytoplasmic C-terminal domain, has been suggested to influence channel assembly and function. In this report, we describe the X-ray crystal structure and electrophysiological properties of a C-terminal domain truncation of the Mycobacterium tuberculosis MscL (MtMscLDeltaC). A crystal structure of MtMscLDeltaC solubilized in the detergent n-dodecyl-beta-D-maltopyranoside reveals the pentameric, closed state-like architecture for the membrane spanning region observed in the previously solved full-length MtMscL. Electrophysiological characterization demonstrates that MtMscLDeltaC retains mechanosensitivity, but with conductance and tension sensitivity more closely resembling full length EcMscL than MtMscL. This study establishes that the C-terminal domain of MtMscL is not required for oligomerization of the full-length channel, but rather influences the tension sensitivity and conductance properties of the channel. The collective picture that emerges from these data is that each MscL channel structure has characteristic features, highlighting the importance of studying multiple homologs. Elucidating a role for the cytoplasmic domain in the Mycobacterium tuberculosis mechanosensitive channel of large conductance.,Herrera N, Maksaev G, Haswell ES, Rees DC Sci Rep. 2018 Oct 1;8(1):14566. doi: 10.1038/s41598-018-32536-6. PMID:30275500 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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