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PDBsum entry 2kdu

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protein metals Protein-protein interface(s) links
Metal binding protein/exocytosis PDB id
2kdu
Jmol
Contents
Protein chains
148 a.a. *
36 a.a. *
Metals
_CA ×4
* Residue conservation analysis
PDB id:
2kdu
Name: Metal binding protein/exocytosis
Title: Structural basis of the munc13-1/ca2+-calmodulin interaction: a novel 1-26 calmodulin binding motif with a bipartite binding mode
Structure: Calmodulin. Chain: a. Synonym: cam. Engineered: yes. Protein unc-13 homolog a. Chain: b. Fragment: unp residues 458-492, calmodulin binding domain. Synonym: munc13-1. Engineered: yes
Source: Xenopus laevis. Clawed frog,common platanna,platanna. Organism_taxid: 8355. Gene: calm1, calm2. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes
NMR struc: 20 models
Authors: F.A.Rodriguez-Castaneda,M.Maestre-Martinez,N.Coudevylle, K.Dimova,O.Jahn,H.Junge,S.Becker,N.Brose,T.Carlomagno, C.Griesinger
Key ref: F.Rodríguez-Castañeda et al. (2010). Modular architecture of Munc13/calmodulin complexes: dual regulation by Ca2+ and possible function in short-term synaptic plasticity. EMBO J, 29, 680-691. PubMed id: 20010694
Date:
19-Jan-09     Release date:   15-Dec-09    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P62155  (CALM_XENLA) -  Calmodulin
Seq:
Struc:
149 a.a.
148 a.a.
Protein chain
Pfam   ArchSchema ?
Q62768  (UN13A_RAT) -  Protein unc-13 homolog A
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1735 a.a.
36 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biochemical function     protein binding     4 terms  

 

 
EMBO J 29:680-691 (2010)
PubMed id: 20010694  
 
 
Modular architecture of Munc13/calmodulin complexes: dual regulation by Ca2+ and possible function in short-term synaptic plasticity.
F.Rodríguez-Castañeda, M.Maestre-Martínez, N.Coudevylle, K.Dimova, H.Junge, N.Lipstein, D.Lee, S.Becker, N.Brose, O.Jahn, T.Carlomagno, C.Griesinger.
 
  ABSTRACT  
 
Ca(2+) signalling in neurons through calmodulin (CaM) has a prominent function in regulating synaptic vesicle trafficking, transport, and fusion. Importantly, Ca(2+)-CaM binds a conserved region in the priming proteins Munc13-1 and ubMunc13-2 and thus regulates synaptic neurotransmitter release in neurons in response to residual Ca(2+) signals. We solved the structure of Ca(2+)(4)-CaM in complex with the CaM-binding domain of Munc13-1, which features a novel 1-5-8-26 CaM-binding motif with two separated mobile structural modules, each involving a CaM domain. Photoaffinity labelling data reveal the same modular architecture in the complex with the ubMunc13-2 isoform. The N-module can be dissociated with EGTA to form the half-loaded Munc13/Ca(2+)(2)-CaM complex. The Ca(2+) regulation of these Munc13 isoforms can therefore be explained by the modular nature of the Munc13/Ca(2+)-CaM interactions, where the C-module provides a high-affinity interaction activated at nanomolar [Ca(2+)](i), whereas the N-module acts as a sensor at micromolar [Ca(2+)](i). This Ca(2+)/CaM-binding mode of Munc13 likely constitutes a key molecular correlate of the characteristic Ca(2+)-dependent modulation of short-term synaptic plasticity.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21353526 D.Fioravante, and W.G.Regehr (2011).
Short-term forms of presynaptic plasticity.
  Curr Opin Neurobiol, 21, 269-274.  
21143597 R.Martín, D.Bartolomé-Martín, M.Torres, and J.Sánchez-Prieto (2011).
Non-additive potentiation of glutamate release by phorbol esters and metabotropic mGlu7 receptor in cerebrocortical nerve terminals.
  J Neurochem, 116, 476-485.  
20370319 T.Mittelstaedt, E.Alvaréz-Baron, and S.Schoch (2010).
RIM proteins and their role in synapse function.
  Biol Chem, 391, 599-606.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.