 |
PDBsum entry 4fbz
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Membrane protein
|
PDB id
|
|
|
|
4fbz
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Crystal structure of deltarhodopsin-3 from haloterrigena thermotolerans.
|
|
|
Authors
|
|
J.Zhang,
K.Mizuno,
Y.Murata,
H.Koide,
M.Murakami,
K.Ihara,
T.Kouyama.
|
|
|
Ref.
|
|
Proteins, 2013,
81,
1585-1592.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
Deltarhodopsin, a new member of the microbial rhodopsin family, functions as a
light-driven proton pump. Here, we report the three-dimensional structure of
deltarhodopsin (dR3) from Haloterrigena thermotolerans at 2.7 Å resolution. A
crystal belonging to space group R32 (a, b = 111.71 Å, c = 198.25 Å) was
obtained by the membrane fusion method. In this crystal, dR3 forms a trimeric
structure as observed for bacteriorhodopsin (bR). Structural comparison of dR
with bR showed that the inner part (the proton release and uptake pathways) is
highly conserved. Meanwhile, residues in the protein-protein contact region are
largely altered so that the diameter of the trimeric structure at the
cytoplasmic side is noticeably larger in dR3. Unlike bR, dR3 possesses a helical
segment at the C-terminal region that fills the space between the AB and EF
loops. A significant difference is also seen in the FG loop, which is one
residue longer in dR3. Another peculiar property of dR3 is a highly crowded
distribution of positively charged residues on the cytoplasmic surface, which
may be relevant to a specific interaction with some cytoplasmic
component.Proteins 2013; © 2013 Wiley Periodicals, Inc.
|
|
|
|
|
|
|
