Crystal structure of YetJ from Bacillus Subtilis at pH 6 by soakingCrystal structure of YetJ from Bacillus Subtilis at pH 6 by soaking

Structural highlights

4pgs is a 1 chain structure with sequence from Bacillus subtilis subsp. subtilis str. 168. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.5Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

YETJ_BACSU

Publication Abstract from PubMed

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.

Structural basis for a pH-sensitive calcium leak across membranes.,Chang Y, Bruni R, Kloss B, Assur Z, Kloppmann E, Rost B, Hendrickson WA, Liu Q Science. 2014 Jun 6;344(6188):1131-5. doi: 10.1126/science.1252043. PMID:24904158[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Chang Y, Bruni R, Kloss B, Assur Z, Kloppmann E, Rost B, Hendrickson WA, Liu Q. Structural basis for a pH-sensitive calcium leak across membranes. Science. 2014 Jun 6;344(6188):1131-5. doi: 10.1126/science.1252043. PMID:24904158 doi:http://dx.doi.org/10.1126/science.1252043

4pgs, resolution 2.50Å

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