Database accession: MF7000462
Name: EhpR from Enterobacter agglomerans
PDB ID: 3sk2
Experimental method: X-ray (1.01 Å)
Assembly: Homodimer
Source organism: Enterobacter agglomerans
Primary publication of the structure:
Yu S, Vit A, Devenish S, Mahanty HK, Itzen A, Goody RS, Blankenfeldt W
Atomic resolution structure of EhpR: phenazine resistance in Enterobacter agglomerans Eh1087 follows principles of bleomycin/mitomycin C resistance in other bacteria.
(2011) BMC Struct. Biol. 11: 33
PMID: 21849072
Abstract:
Not available.
Annotations from the GeneOntology database. Only terms that fit at least two of the interacting proteins are shown. Molecular function:
organic acid binding organic acid binding
protein homodimerization activity protein homodimerization activity
Biological process:
response to antibiotic response to antibiotic
Cellular component: not assigned
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
Name: Phenazine antibiotic resistance protein EhpR
Source organism: Enterobacter agglomerans
Length: 129 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMTDLAGPTITPNLQLVYVSNVERSTDFYRFIFKKEPVFVTPRYVAFPSSGDALFAIWSGGEEPVAEIPRFSEIGIMLPTGEDVDKLFNEWTKQKSHQIIVIKEPYTDVFGRTFLISDPDGHIIRVCPLD
UniProtKB AC: Q8GPH6 (positions: 1-129)
Coverage: 100%
Name: Phenazine antibiotic resistance protein EhpR
Source organism: Enterobacter agglomerans
Length: 129 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMTDLAGPTITPNLQLVYVSNVERSTDFYRFIFKKEPVFVTPRYVAFPSSGDALFAIWSGGEEPVAEIPRFSEIGIMLPTGEDVDKLFNEWTKQKSHQIIVIKEPYTDVFGRTFLISDPDGHIIRVCPLD
UniProtKB AC: Q8GPH6 (positions: 1-129)
Coverage: 100%
Evidence demonstrating that the participating proteins are unstructured prior to the interaction and their folding is coupled to binding. Representative domain in related structures: Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily
Evidence level: Indirect evidence
Evidence coverage: The full structure participates in mutual synergistic folding.
Complex Evidence:
The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648).
Chain A:
N/A
Chain B:
N/A
Surface and contacts features:
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). Download the CIF file (.cif)
Download this entry's XML file (.xml)
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