General Information

Database accession: MF7000581

Name: Ca2+-bound Calcyclin

PDB ID: 1a03 PDBe

Experimental method: NMR

Assembly: Homodimer

Source organism: Oryctolagus cuniculus

Primary publication of the structure:

Sastry M, Ketchem RR, Crescenzi O, Weber C, Lubienski MJ, Hidaka H, Chazin WJ
The three-dimensional structure of Ca(2+)-bound calcyclin: implications for Ca(2+)-signal transduction by S100 proteins.
(1998) Structure 6: 223-31

PMID: 9519412 PubMed

Abstract:

Not available.


Function and Biology Annotations from the GeneOntology database. Only terms that fit at least two of the interacting proteins are shown.

Molecular function:

calcium ion binding calcium ion binding GeneOntology

calcium-dependent protein binding calcium-dependent protein binding GeneOntology

S100 protein binding S100 protein binding GeneOntology

Biological process: not assigned

Cellular component:

collagen-containing extracellular matrix collagen-containing extracellular matrix GeneOntology

cytoplasmic side of plasma membrane cytoplasmic side of plasma membrane GeneOntology

cytosol cytosol GeneOntology

extracellular space extracellular space GeneOntology

nuclear envelope nuclear envelope GeneOntology

perinuclear region of cytoplasm perinuclear region of cytoplasm GeneOntology

Structure Summary Structural annotations of the participating protein chains.

Entry contents: 2 distinct polypeptide molecules

Chains: A, B

Notes: All chains according to the most probable oligomerization state stored in PDBe were considered.

Number of unique protein segments: 1


Chain A

Name: Protein S100-A6

Source organism: Oryctolagus cuniculus

Length: 90 residues

Sequence:Sequence according to the corresponding UniProt protein segmentMASPLDQAIGLLIGIFHKYSGKEGDKHTLSKKELKELIQKELTIGSKLQDAEIVKLMDDLDRNKDQEVNFQEYITFLGALAMIYNEALKG

UniProtKB AC: P30801 (positions: 1-90) UniProt

Coverage: 100%

Chain B

Name: Protein S100-A6

Source organism: Oryctolagus cuniculus

Length: 90 residues

Sequence:Sequence according to the corresponding UniProt protein segmentMASPLDQAIGLLIGIFHKYSGKEGDKHTLSKKELKELIQKELTIGSKLQDAEIVKLMDDLDRNKDQEVNFQEYITFLGALAMIYNEALKG

UniProtKB AC: P30801 (positions: 1-90) UniProt

Coverage: 100%

Evidence Evidence demonstrating that the participating proteins are unstructured prior to the interaction and their folding is coupled to binding.

Representative domain in related structures: S-100/ICaBP type EF hand dimer

Evidence level: Direct evidence

Evidence coverage: The full structure participates in mutual synergistic folding.

Complex Evidence:

GuHCl-induced denaturation of the S100B protein dimer showed that it follows a two-state unfolding/refolding process (PMID:11888280). Other S100 proteins also showed two-state unfolding, no folded monomers were observed (PMID:18346834, PMID:18706914). The dimer has a globular and compact structure with the four helices in each subunit aligning to form a unicornate-type four-helix bundle (PMID:11790100). The hydrophobic core extends through the dimer interface.

Chain A:

N/A

Chain B:

N/A

Surface and contacts features:

Related Structure(s) Structures from the PDB that contain the same number of proteins, and the proteins from the two structures show a sufficient degree of pairwise similarity, i.e. they belong to the same UniRef90 cluster (the full proteins exhibit at least 90% sequence identity) and convey roughly the same region to their respective interactions (the two regions from the two proteins share a minimum of 70% overlap).

There are 37 related structures in the MFIB database:






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