This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

4p60

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 20:34, 4 August 2016

Structure of the N-terminal domain of the human mitochondrial aspartate/glutamate carrier Aralar in the apo state

Structural highlights

4p60 is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	4p5x
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[CMC1_HUMAN] Epileptic encephalopathy with global cerebral demyelination. The disease is caused by mutations affecting the gene represented in this entry.

Function

[CMC1_HUMAN] Catalyzes the calcium-dependent exchange of cytoplasmic glutamate with mitochondrial aspartate across the mitochondrial inner membrane. May have a function in the urea cycle.^[1]

Publication Abstract from PubMed

The transport activity of human mitochondrial aspartate/glutamate carriers is central to the malate-aspartate shuttle, urea cycle, gluconeogenesis and myelin synthesis. They have a unique three-domain structure, comprising a calcium-regulated N-terminal domain with eight EF-hands, a mitochondrial carrier domain, and a C-terminal domain. Here we present the calcium-bound and calcium-free structures of the N- and C-terminal domains, elucidating the mechanism of calcium regulation. Unexpectedly, EF-hands 4-8 are involved in dimerization of the carrier and form a static unit, whereas EF-hands 1-3 form a calcium-responsive mobile unit. On calcium binding, an amphipathic helix of the C-terminal domain binds to the N-terminal domain, opening a vestibule. In the absence of calcium, the mobile unit closes the vestibule. Opening and closing of the vestibule might regulate access of substrates to the carrier domain, which is involved in their transport. These structures provide a framework for understanding cases of the mitochondrial disease citrin deficiency.

Calcium-induced conformational changes of the regulatory domain of human mitochondrial aspartate/glutamate carriers.,Thangaratnarajah C, Ruprecht JJ, Kunji ER Nat Commun. 2014 Nov 20;5:5491. doi: 10.1038/ncomms6491. PMID:25410934^[2]

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

References

↑ Palmieri L, Pardo B, Lasorsa FM, del Arco A, Kobayashi K, Iijima M, Runswick MJ, Walker JE, Saheki T, Satrustegui J, Palmieri F. Citrin and aralar1 are Ca(2+)-stimulated aspartate/glutamate transporters in mitochondria. EMBO J. 2001 Sep 17;20(18):5060-9. PMID:11566871 doi:http://dx.doi.org/10.1093/emboj/20.18.5060
↑ Thangaratnarajah C, Ruprecht JJ, Kunji ER. Calcium-induced conformational changes of the regulatory domain of human mitochondrial aspartate/glutamate carriers. Nat Commun. 2014 Nov 20;5:5491. doi: 10.1038/ncomms6491. PMID:25410934 doi:http://dx.doi.org/10.1038/ncomms6491

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4p60"

Categories: Kunji, E R.S | Ruprecht, J J | Thangaratnarajah, C | Transport protein

@@ Line 1: / Line 1: @@
 ==Structure of the N-terminal domain of the human mitochondrial aspartate/glutamate carrier Aralar in the apo state==
 <StructureSection load='4p60' size='340' side='right' caption='[[4p60]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4p5x|4p5x]]</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=4p60 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p60 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4p60 RCSB], [http://www.ebi.ac.uk/pdbsum/4p60 PDBsum]</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=4p60 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p60 OCA], [http://pdbe.org/4p60 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4p60 RCSB], [http://www.ebi.ac.uk/pdbsum/4p60 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4p60 ProSAT]</span></td></tr>
 </table>
 == Disease ==
@@ Line 19: / Line 20: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4p60" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

4p60

From Proteopedia

Revision as of 20:34, 4 August 2016

Structure of the N-terminal domain of the human mitochondrial aspartate/glutamate carrier Aralar in the apo state

Structural highlights

Disease

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox