4n5x
From Proteopedia
(Difference between revisions)
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| - | + | ==Crystal structure of N-terminal calmodulin-like Calcium sensor of human mitochondrial ATP-Mg/Pi carrier SCaMC1== | |
| - | + | <StructureSection load='4n5x' size='340' side='right' caption='[[4n5x]], [[Resolution|resolution]] 2.10Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4n5x]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4N5X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4N5X FirstGlance]. <br> | |
| - | ==Function== | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr> |
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SLC25A24, APC1, MCSC1, SCAMC1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4n5x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n5x OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4n5x RCSB], [http://www.ebi.ac.uk/pdbsum/4n5x PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
[[http://www.uniprot.org/uniprot/SCMC1_HUMAN 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.<ref>PMID:15123600</ref> | [[http://www.uniprot.org/uniprot/SCMC1_HUMAN 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.<ref>PMID:15123600</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The mitochondrial carriers play essential roles in energy metabolism. The short Ca(2+)-binding mitochondrial carrier (SCaMC) transports ATP-Mg in exchange for Pi and is important for activities that depend on adenine nucleotides. SCaMC adopts, in addition to the transmembrane domain (TMD) that transports solutes, an extramembrane N-terminal domain (NTD) that regulates solute transport in a Ca(2+)-dependent manner. Crystal structure of the Ca(2+)-bound NTD reveals a compact architecture in which the functional EF hands are sequestered by an endogenous helical segment. Nuclear magnetic resonance (NMR) relaxation rates indicated that removal of Ca(2+) from NTD results in a major conformational switch from the rigid and compact Ca(2+)-bound state to the dynamic and loose apo state. Finally, we showed using surface plasmon resonance and NMR titration experiments that free apo NTDs could specifically interact with liposome-incorporated TMD, but that Ca(2+) binding drastically weakened the interaction. Our results together provide a molecular explanation for Ca(2+)-dependent ATP-Mg flux in mitochondria. | ||
| - | + | A Self-Sequestered Calmodulin-like Ca(2+) Sensor of Mitochondrial SCaMC Carrier and Its Implication to Ca(2+)-Dependent ATP-Mg/Pi Transport.,Yang Q, Bruschweiler S, Chou JJ Structure. 2014 Feb 4;22(2):209-17. doi: 10.1016/j.str.2013.10.018. Epub 2013 Dec, 12. PMID:24332718<ref>PMID:24332718</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| - | [[Category: Bruschweiler, S | + | == References == |
| - | [[Category: Chou, J | + | <references/> |
| - | [[Category: Yang, Q | + | __TOC__ |
| + | </StructureSection> | ||
| + | [[Category: Human]] | ||
| + | [[Category: Bruschweiler, S]] | ||
| + | [[Category: Chou, J]] | ||
| + | [[Category: Yang, Q]] | ||
[[Category: Calcium sensor]] | [[Category: Calcium sensor]] | ||
[[Category: Calcium-binding protein]] | [[Category: Calcium-binding protein]] | ||
[[Category: Calmodulin]] | [[Category: Calmodulin]] | ||
[[Category: Mitochondrial inner membrane]] | [[Category: Mitochondrial inner membrane]] | ||
Revision as of 09:25, 25 December 2014
Crystal structure of N-terminal calmodulin-like Calcium sensor of human mitochondrial ATP-Mg/Pi carrier SCaMC1
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