TCDB is operated by the Saier Lab Bioinformatics Group
« See all members of the family


1.A.22.1.11
Large conductance mechanosensitive channel protein, MscL, of 101 aas and 2 TMSs. 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. The structures of this archaeal MscL, trapped in the closed and expanded intermediate states, has been solved (Li et al. 2015). 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 (TMS1 and TMS2) fit well with the helix-pivoting model. 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 TMS1 and TMS2. The dynamic relationships between the N-helix and TMS1/TMS2 suggest that the N-helix serves as a membrane-anchored stopper that limits the tilts of TM1 and TM2 in the gating process (Li et al. 2015).

Accession Number:Q8TNK0
Protein Name:Large conductance mechanosensitive channel protein
Length:101
Molecular Weight:11183.00
Species:Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A) [188937]
Number of TMSs:2
Substrate ions

Cross database links:

Structure:
4Y7J   4Y7K     

External Searches:

  • Search: DB with
  • BLAST ExPASy (Swiss Institute of Bioinformatics (SIB) BLAST)
  • CDD Search (Conserved Domain Database)
  • Search COGs (Clusters of Orthologous Groups of proteins)
  • 2° Structure (Network Protein Sequence Analysis)

Analyze:

Predict TMSs (Predict number of transmembrane segments)
Window Size: Angle:  
Window Size: Angle:  
FASTA formatted sequence
1:	MGLFSEFKEF LYEYKVIPLA IAFIMGIAST ALIKSFVDNI IMPIITPFVP GGGWETATVE 
61:	LGPIVISWGA FLGELVNFII IAFAVFIIAK KVLQEEKVEK K