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4n5x

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Revision as of 10:37, 28 December 2022

Crystal structure of N-terminal calmodulin-like Calcium sensor of human mitochondrial ATP-Mg/Pi carrier SCaMC1

Structural highlights

4n5x is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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]

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^[2]

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

References

↑ 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
↑ 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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4n5x"

Categories: Homo sapiens | Large Structures | Bruschweiler S | Chou J | Yang Q

@@ Line 1: / Line 1: @@
 ==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]] 2.10&Aring;' scene=''>
+<StructureSection load='4n5x' size='340' side='right'caption='[[4n5x]], [[Resolution|resolution]] 2.10&Aring;' 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>
+<table><tr><td colspan='2'>[[4n5x]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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 [https://proteopedia.org/fgij/fg.htm?mol=4N5X FirstGlance]. <br>
-</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>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[https://proteopedia.org/fgij/fg.htm?mol=4n5x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n5x OCA], [https://pdbe.org/4n5x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4n5x RCSB], [https://www.ebi.ac.uk/pdbsum/4n5x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4n5x ProSAT]</span></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://pdbe.org/4n5x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4n5x RCSB], [http://www.ebi.ac.uk/pdbsum/4n5x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4n5x ProSAT]</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>
+[https://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 ==
@@ Line 23: / Line 22: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
-[[Category: Bruschweiler, S]]
+[[Category: Large Structures]]
-[[Category: Chou, J]]
+[[Category: Bruschweiler S]]
-[[Category: Yang, Q]]
+[[Category: Chou J]]
-[[Category: Calcium sensor]]
+[[Category: Yang Q]]
-[[Category: Calcium-binding protein]]
-[[Category: Calmodulin]]
-[[Category: Mitochondrial inner membrane]]

4n5x

From Proteopedia

Revision as of 10:37, 28 December 2022

Crystal structure of N-terminal calmodulin-like Calcium sensor of human mitochondrial ATP-Mg/Pi carrier SCaMC1

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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