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Calcium-induced conformational changes in the regulatory domain of the human mitochondrial ATP-Mg/Pi carrier.

Harborne SP, Ruprecht JJ, Kunji ER - Biochim. Biophys. Acta (2015)

Bottom Line: Careful analysis by SEC confirmed that although the regulatory domain crystallised as dimers, full-length ATP-Mg/Pi carrier is monomeric.Detailed bioinformatics analyses of different EF-hand states indicate that upon release of calcium, EF-hands close, meaning that the regulatory domain would release the amphipathic α-helix.We propose a mechanism for ATP-Mg/Pi carriers in which the amphipathic α-helix becomes mobile upon release of calcium and could block the transport of substrates across the mitochondrial inner membrane.

View Article: PubMed Central - PubMed

Affiliation: The Medical Research Council, Mitochondrial Biology Unit, Cambridge Biomedical Campus, Wellcome Trust/MRC Building, Hills Road, Cambridge CB2 0XY, UK.

No MeSH data available.


Calcium-induced conformational changes in EF-hands.Views of 129 EF-hands superposed on EF-hand 1 of calcium-bound calmodulin, in the calcium-free (A–C) and calcium-bound (D–F) states. Entering and exiting α-helices are represented as a line though the α-helix centre. G) A histogram of the angles between the entering and exiting α-helices of conventional (not S100-like) EF-hands.
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f0020: Calcium-induced conformational changes in EF-hands.Views of 129 EF-hands superposed on EF-hand 1 of calcium-bound calmodulin, in the calcium-free (A–C) and calcium-bound (D–F) states. Entering and exiting α-helices are represented as a line though the α-helix centre. G) A histogram of the angles between the entering and exiting α-helices of conventional (not S100-like) EF-hands.

Mentions: Calcium-bound EF-hands displayed open or semi-open conformations. The angle of the exiting α-helix relative to the entering α-helix was 70° to 90° and 55° to 70°, respectively (Fig. 4). Calcium-free EF-hands displayed generally a closed conformation (45° to 65°). These results agree with a previous study [52], but expand the reference set to include a larger number of EF-hands published since the previous study was conducted.


Calcium-induced conformational changes in the regulatory domain of the human mitochondrial ATP-Mg/Pi carrier.

Harborne SP, Ruprecht JJ, Kunji ER - Biochim. Biophys. Acta (2015)

Calcium-induced conformational changes in EF-hands.Views of 129 EF-hands superposed on EF-hand 1 of calcium-bound calmodulin, in the calcium-free (A–C) and calcium-bound (D–F) states. Entering and exiting α-helices are represented as a line though the α-helix centre. G) A histogram of the angles between the entering and exiting α-helices of conventional (not S100-like) EF-hands.
© Copyright Policy - CC BY
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4562336&req=5

f0020: Calcium-induced conformational changes in EF-hands.Views of 129 EF-hands superposed on EF-hand 1 of calcium-bound calmodulin, in the calcium-free (A–C) and calcium-bound (D–F) states. Entering and exiting α-helices are represented as a line though the α-helix centre. G) A histogram of the angles between the entering and exiting α-helices of conventional (not S100-like) EF-hands.
Mentions: Calcium-bound EF-hands displayed open or semi-open conformations. The angle of the exiting α-helix relative to the entering α-helix was 70° to 90° and 55° to 70°, respectively (Fig. 4). Calcium-free EF-hands displayed generally a closed conformation (45° to 65°). These results agree with a previous study [52], but expand the reference set to include a larger number of EF-hands published since the previous study was conducted.

Bottom Line: Careful analysis by SEC confirmed that although the regulatory domain crystallised as dimers, full-length ATP-Mg/Pi carrier is monomeric.Detailed bioinformatics analyses of different EF-hand states indicate that upon release of calcium, EF-hands close, meaning that the regulatory domain would release the amphipathic α-helix.We propose a mechanism for ATP-Mg/Pi carriers in which the amphipathic α-helix becomes mobile upon release of calcium and could block the transport of substrates across the mitochondrial inner membrane.

View Article: PubMed Central - PubMed

Affiliation: The Medical Research Council, Mitochondrial Biology Unit, Cambridge Biomedical Campus, Wellcome Trust/MRC Building, Hills Road, Cambridge CB2 0XY, UK.

No MeSH data available.