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4n5x
From Proteopedia
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{{STRUCTURE_4n5x| PDB=4n5x | SCENE= }} | {{STRUCTURE_4n5x| PDB=4n5x | SCENE= }} | ||
===Crystal structure of N-terminal calmodulin-like Calcium sensor of human mitochondrial ATP-Mg/Pi carrier SCaMC1=== | ===Crystal structure of N-terminal calmodulin-like Calcium sensor of human mitochondrial ATP-Mg/Pi carrier SCaMC1=== | ||
| + | {{ABSTRACT_PUBMED_24332718}} | ||
==Function== | ==Function== | ||
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==Reference== | ==Reference== | ||
| - | <references group="xtra"/><references/> | + | <ref group="xtra">PMID:024332718</ref><references group="xtra"/><references/> |
[[Category: Bruschweiler, S.]] | [[Category: Bruschweiler, S.]] | ||
[[Category: Chou, J.]] | [[Category: Chou, J.]] | ||
Revision as of 14:30, 3 March 2014
Contents |
Crystal structure of N-terminal calmodulin-like Calcium sensor of human mitochondrial ATP-Mg/Pi carrier SCaMC1
Template:ABSTRACT PUBMED 24332718
Function
[SCMC1_HUMAN] Calcium-dependent mitochondrial solute carrier. Mitochondrial solute carriers shuttle metabolites, nucleotides, and cofactors through the mitochondrial inner membrane. May act as a ATP-Mg/Pi exchanger that mediates the transport of Mg-ATP in exchange for phosphate, catalyzing the net uptake or efflux of adenine nucleotides into or from the mitochondria.[1]
About this Structure
4n5x is a 1 chain structure. Full crystallographic information is available from OCA.
Reference
- Yang Q, Bruschweiler S, Chou JJ. A Self-Sequestered Calmodulin-like Ca(2+) Sensor of Mitochondrial SCaMC Carrier and Its Implication to Ca(2+)-Dependent ATP-Mg/Pi Transport. Structure. 2014 Feb 4;22(2):209-17. doi: 10.1016/j.str.2013.10.018. Epub 2013 Dec, 12. PMID:24332718 doi:http://dx.doi.org/10.1016/j.str.2013.10.018
- ↑ Fiermonte G, De Leonardis F, Todisco S, Palmieri L, Lasorsa FM, Palmieri F. Identification of the mitochondrial ATP-Mg/Pi transporter. Bacterial expression, reconstitution, functional characterization, and tissue distribution. J Biol Chem. 2004 Jul 16;279(29):30722-30. Epub 2004 Apr 29. PMID:15123600 doi:http://dx.doi.org/10.1074/jbc.M400445200
