General Information

Database accession: MF7000613

Name: Murine S100A7/S100A15

PDB ID: 8s9w PDBe

Experimental method: X-ray (1.69 Å)

Assembly: Homodimer

Source organism: Mus musculus

Primary publication of the structure:

Harrison, S.A., Naretto, A., Balakrishnan, S., Perera, Y.R., Chazin, W.J.
Comparative analysis of the physical properties of murine and human S100A7: Insight into why zinc piracy is mediated by human but not murine S100A7.
(2023) J. Biol. Chem. 299: 105292-105292

PMID: 37769710 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

chemoattractant activity chemoattractant activity GeneOntology

transition metal ion binding transition metal ion binding GeneOntology

Biological process:

inflammatory response inflammatory response GeneOntology

Cellular component:

cytoplasm cytoplasm GeneOntology

extracellular space extracellular space 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-A15A

Source organism: Mus musculus

Length: 108 residues

Sequence:Sequence according to the corresponding UniProt protein segmentMPDTPVEDSLFQIIHCFHHYAAREGDKETLSLEELKALLLDSVPRFMDTLGRRQPYYITELFRAADKNKDNQICFDEFLYILGKLVKDYHLQFHRQLCAHYCTEHSLY

UniProtKB AC: Q6S5I3 (positions: 2-99) UniProt

Coverage: 90%

Chain B

Name: Protein S100-A15A

Source organism: Mus musculus

Length: 108 residues

Sequence:Sequence according to the corresponding UniProt protein segmentMPDTPVEDSLFQIIHCFHHYAAREGDKETLSLEELKALLLDSVPRFMDTLGRRQPYYITELFRAADKNKDNQICFDEFLYILGKLVKDYHLQFHRQLCAHYCTEHSLY

UniProtKB AC: Q6S5I3 (positions: 2-95) UniProt

Coverage: 87%

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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