 |
PDBsum entry 4pgv
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
|
|
|
|
|
|
|
|
|
Membrance protein
|
PDB id
|
|
|
|
4pgv
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
 |
|
Key reference
|
 |
|
Title
|
 |
Structural basis for a ph-Sensitive calcium leak across membranes.
|
 |
|
Authors
|
 |
Y.Chang,
R.Bruni,
B.Kloss,
Z.Assur,
E.Kloppmann,
B.Rost,
W.A.Hendrickson,
Q.Liu.
|
 |
|
Ref.
|
 |
Science, 2014,
344,
1131-1135.
[DOI no: ]
|
 |
|
PubMed id
|
 |
|
 |
|
Note: In the PDB file this reference is
annotated as "TO BE PUBLISHED". The citation details given above have
been manually determined.
|
 |
 |
|
Abstract
|
 |
|
Calcium homeostasis balances passive calcium leak and active calcium uptake.
Human Bax inhibitor-1 (hBI-1) is an antiapoptotic protein that mediates a
calcium leak and is representative of a highly conserved and widely distributed
family, the transmembrane Bax inhibitor motif (TMBIM) proteins. Here, we present
crystal structures of a bacterial homolog and characterize its calcium leak
activity. The structure has a seven-transmembrane-helix fold that features two
triple-helix sandwiches wrapped around a central C-terminal helix. Structures
obtained in closed and open conformations are reversibly interconvertible by
change of pH. A hydrogen-bonded, pKa (where Ka is the acid dissociation
constant)-perturbed pair of conserved aspartate residues explains the pH
dependence of this transition, and biochemical studies show that pH regulates
calcium influx in proteoliposomes. Homology models for hBI-1 provide insights
into TMBIM-mediated calcium leak and cytoprotective activity.
|
 |
|
|
|
|
 |