General Information

Database accession: MF7000156

Name: Multiple antibiotic-resistance repressor (MarR) from Xanthomonas campestris

PDB ID: 2fa5 PDBe

Experimental method: X-ray (1.80 Å)

Assembly: Homodimer

Source organism: Xanthomonas campestris pv campestris

Primary publication of the structure:

Chin KH, Tu ZL, Li JN, Chou CC, Wang AH, Chou SH
The crystal structure of XC1739: a putative multiple antibiotic-resistance repressor (MarR) from Xanthomonas campestris at 1.8 A resolution.
(2006) Proteins 65: 239-42

PMID: 16862595 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:

DNA binding DNA binding GeneOntology

DNA-binding transcription factor activity DNA-binding transcription factor activity GeneOntology

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 regulator marR/emrR family

Source organism: Xanthomonas campestris pv campestris

Length: 162 residues

Sequence:Sequence according to the corresponding UniProt protein segmentMSDLDTPTPSPHPVLLNLEQFLPYRLSVLSNRISGNIAKVYGDRYGMAIPEWRVITILALYPGSSASEVSDRTAMDKVAVSRAVARLLERGFIRRETHGDDRRRSMLALSPAGRQVYETVAPLVNEMEQRLMSVFSAEEQQTLERLIDRLAKDGLPRMASKD

UniProtKB AC: Q8PDA5 (positions: 12-159) UniProt

Coverage: 91%

Chain B

Name: Transcriptional regulator marR/emrR family

Source organism: Xanthomonas campestris pv campestris

Length: 162 residues

Sequence:Sequence according to the corresponding UniProt protein segmentMSDLDTPTPSPHPVLLNLEQFLPYRLSVLSNRISGNIAKVYGDRYGMAIPEWRVITILALYPGSSASEVSDRTAMDKVAVSRAVARLLERGFIRRETHGDDRRRSMLALSPAGRQVYETVAPLVNEMEQRLMSVFSAEEQQTLERLIDRLAKDGLPRMASKD

UniProtKB AC: Q8PDA5 (positions: 10-159) UniProt

Coverage: 92%

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 (MarR type II) transcriptional regulator

Evidence level: Indirect evidence

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

Complex Evidence:

Thermal unfolding measured with circular dichroism of the MarR family protein, HucR, suggested two-state model of unfolding (PMID:15448166). Also, a decrease in pH induced a molten globule-like state, where the protein remained in dimeric form (PMID:27282811). Helices 1, 2, 6 and 7 form the dimerization subdomain, they form an apparently stable dimer interface that preconfigures the DNA recognition HTH subdomain for DNA binding (PMID:16750221).

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 11 related structures in the MFIB database:






The molecule viewer shows our modified stucture.

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