Sandbox: Difference between revisions

From Proteopedia
Jump to navigationJump to search
No edit summary
No edit summary
Line 55: Line 55:
'''Key Structural Characteristics:'''
'''Key Structural Characteristics:'''
#'''Overall Fold:'''
#'''Overall Fold:'''
:*Adopts the classic Major Facilitator Superfamily (MFS) fold.
::*Adopts the classic Major Facilitator Superfamily (MFS) fold.


:Comprises 12 transmembrane helices (TMs 1-12).
::*Comprises 12 transmembrane helices (TMs 1-12).


:Exhibits pseudo-two-fold symmetry, divided into an N-lobe (TMs 1-6) and a C-lobe (TMs 7-12).
::*Exhibits pseudo-two-fold symmetry, divided into an N-lobe (TMs 1-6) and a C-lobe (TMs 7-12).
 
#'''Central Binding Cavity:'''
 
::*The cavity is located between the N-lobe (formed by TM1, TM2, TM4, TM5) and the C-lobe (formed by TM7, TM8, TM10, TM11).
 
::*It possesses a positively charged electrostatic environment, which explains its strong preference for transporting anionic substrates.
 
::*The cavity is lined by 29 residues, forming a hydrophobic and aromatic-rich environment.
 
#'''Cavity Borders and Cytosolic Gate:'''
 
::*The top border (extracellular side) of the cavity is formed by residues including N35, Y230, Y353, and Y354.
 
::*The bottom border (cytosolic side) features a narrow "thin bottom gate" formed by residues M207 and F442. The interaction between these two residues splits the cytosolic entrance into two distinct pathways:
 
:::*Path A: Located between TM2 and TM11.
 
:::*Path B: Located between TM5 and TM8.
 
#'''Conformational State:'''
 
::*In the apo state, the transporter is in a relaxed, inward-open conformation, providing access for substrates from the cytoplasm.
 
::*The structure serves as a baseline for understanding the conformational changes that occur upon substrate or inhibitor binding.


===OmcS Structure===
===OmcS Structure===