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PDBsum entry 4nsc

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protein Protein-protein interface(s) links
Calcium binding protein PDB id
4nsc

 

 

 

 

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Contents
Protein chains
310 a.a.
316 a.a.
330 a.a.
330 a.a.
Waters ×13
PDB id:
4nsc
Name: Calcium binding protein
Title: Crystal structure of cbara1 in the apo-form
Structure: Calcium uptake protein 1, mitochondrial. Chain: a, b, c, d, e, f. Fragment: unp residues 97-476. Synonym: atopy-related autoantigen calc, ara calc, calcium-binding atopy-related autoantigen 1. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: micu1, calc, cbara1. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
3.20Å     R-factor:   0.254     R-free:   0.307
Authors: L.Wang,X.Yang,S.Li,Y.Shen
Key ref: L.Wang et al. (2014). Structural and mechanistic insights into MICU1 regulation of mitochondrial calcium uptake. Embo J, 33, 594-604. PubMed id: 24514027 DOI: 10.1002/embj.201386523
Date:
28-Nov-13     Release date:   26-Feb-14    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q9BPX6  (MICU1_HUMAN) -  Calcium uptake protein 1, mitochondrial from Homo sapiens
Seq:
Struc:
476 a.a.
310 a.a.
Protein chains
Pfam   ArchSchema ?
Q9BPX6  (MICU1_HUMAN) -  Calcium uptake protein 1, mitochondrial from Homo sapiens
Seq:
Struc:
476 a.a.
316 a.a.
Protein chains
Pfam   ArchSchema ?
Q9BPX6  (MICU1_HUMAN) -  Calcium uptake protein 1, mitochondrial from Homo sapiens
Seq:
Struc:
476 a.a.
330 a.a.
Protein chain
Pfam   ArchSchema ?
Q9BPX6  (MICU1_HUMAN) -  Calcium uptake protein 1, mitochondrial from Homo sapiens
Seq:
Struc:
476 a.a.
330 a.a.
Key:    PfamA domain  Secondary structure

 

 
DOI no: 10.1002/embj.201386523 Embo J 33:594-604 (2014)
PubMed id: 24514027  
 
 
Structural and mechanistic insights into MICU1 regulation of mitochondrial calcium uptake.
L.Wang, X.Yang, S.Li, Z.Wang, Y.Liu, J.Feng, Y.Zhu, Y.Shen.
 
  ABSTRACT  
 
Mitochondrial calcium uptake is a critical event in various cellular activities. Two recently identified proteins, the mitochondrial Ca(2+) uniporter (MCU), which is the pore-forming subunit of a Ca(2+) channel, and mitochondrial calcium uptake 1 (MICU1), which is the regulator of MCU, are essential in this event. However, the molecular mechanism by which MICU1 regulates MCU remains elusive. In this study, we report the crystal structures of Ca(2+)-free and Ca(2+)-bound human MICU1. Our studies reveal that Ca(2+)-free MICU1 forms a hexamer that binds and inhibits MCU. Upon Ca(2+) binding, MICU1 undergoes large conformational changes, resulting in the formation of multiple oligomers to activate MCU. Furthermore, we demonstrate that the affinity of MICU1 for Ca(2+) is approximately 15-20 μM. Collectively, our results provide valuable details to decipher the molecular mechanism of MICU1 regulation of mitochondrial calcium uptake.
 

 

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