General Information

Database accession: MF7000398

Name: PadR-like transcriptional regulator BC1756

PDB ID: 6jyi PDBe

Experimental method: X-ray (1.92 Å)

Assembly: Homodimer

Source organism: Bacillus cereus

Primary publication of the structure:

Kim TH, Park SC, Lee KC, Song WS, Yoon SI
Structural and DNA-binding studies of the PadR-like transcriptional regulator BC1756 from Bacillus cereus.
(2019) Biochem. Biophys. Res. Commun. :

PMID: 31178139 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: not assigned

Biological process: not assigned

Cellular component: not assigned

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: Transcriptional repressor PadR

Source organism: Bacillus cereus

Length: 179 residues

Sequence:Sequence according to the corresponding UniProt protein segmentMKGRDVVLGLLMQKELSGYDIKIVFEDVFTHFFDGSFGMIYPTLRQLENEGKIKKEVVMQEGKPNKKMYFITDEGREEFYQYMQTPVEKDVLRSDFLMRMYFGNYSDDVTIKKWIKDEIERKEAYIADLRLKYEKWRVGITFVEEISLDVGIASYSAQVETLKKKLEELEAKENNKTEE

UniProtKB AC: Q81F45 (positions: 1-170) UniProt

Coverage: 94%

Chain B

Name: Transcriptional repressor PadR

Source organism: Bacillus cereus

Length: 179 residues

Sequence:Sequence according to the corresponding UniProt protein segmentMKGRDVVLGLLMQKELSGYDIKIVFEDVFTHFFDGSFGMIYPTLRQLENEGKIKKEVVMQEGKPNKKMYFITDEGREEFYQYMQTPVEKDVLRSDFLMRMYFGNYSDDVTIKKWIKDEIERKEAYIADLRLKYEKWRVGITFVEEISLDVGIASYSAQVETLKKKLEELEAKENNKTEE

UniProtKB AC: Q81F45 (positions: 2-173) UniProt

Coverage: 96%

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: Winged helix DNA-binding domain (PadR family) transcriptional regulator

Evidence level: Direct evidence

Evidence coverage: Only some parts of the structure participates in mutual synergistic folding.

Complex Evidence:

AphA monomers were found to be highly unstable (PMID:15647287). AphA is a dimer with an N-terminal winged helix DNA-binding domain and a unique C-terminal antiparallel coiled coil domain that serves as its primary dimerization interface and is a case of mutual synergistic folding (MSF). Another PadR family transcriptional regulator, Rv3488, was shown to be a dimer in solution (PMID:30266832), while differential scanning calorimetry-based thermal denaturation data suggested that the PadR family Rv1176c follows two-state unfolding (PMID:38417748).

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 21 related structures in the MFIB database:






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