Database accession: MF6120001
Name: 4-oxalocrotonate tautomerase
PDB ID: 4x19
Experimental method: X-ray (1.94 Å)
Assembly: Homohexamer
Source organism: Pseudomonas putida
Primary publication of the structure:
Poddar H, Rahimi M, Geertsema EM, Thunnissen AM, Poelarends GJ
Evidence for the formation of an enamine species during aldol and Michael-type addition reactions promiscuously catalyzed by 4-oxalocrotonate tautomerase.
(2015) Chembiochem 16: 738-41
PMID: 25728471
Abstract:
The enzyme 4-oxalocrotonate tautomerase (4-OT), which has a catalytic N-terminal proline residue (Pro1), can promiscuously catalyze various carbon-carbon bond-forming reactions, including aldol condensation of acetaldehyde with benzaldehyde to yield cinnamaldehyde, and Michael-type addition of acetaldehyde to a wide variety of nitroalkenes to yield valuable γ-nitroaldehydes. To gain insight into how 4-OT catalyzes these unnatural reactions, we carried out exchange studies in D2 O, and X-ray crystallography studies. The former established that H-D exchange within acetaldehyde is catalyzed by 4-OT and that the Pro1 residue is crucial for this activity. The latter showed that Pro1 of 4-OT had reacted with acetaldehyde to give an enamine species. These results provide evidence of the mechanism of the 4-OT-catalyzed aldol and Michael-type addition reactions in which acetaldehyde is activated for nucleophilic addition by Pro1-dependent formation of an enamine intermediate.
Annotations from the GeneOntology database. Only terms that fit at least two of the interacting proteins are shown. Molecular function:
isomerase activity isomerase activity
Biological process:
toluene catabolic process toluene catabolic process
xylene catabolic process xylene catabolic process
Cellular component: not assigned
Structural annotations of the participating protein chains.Entry contents: 6 distinct polypeptide molecules
Chains: A, B, C, D, E, F
Notes: All chains according to the most probable oligomerization state stored in PDBe were considered.
Number of unique protein segments: 1
Name: 2-hydroxymuconate tautomerase
Source organism: Pseudomonas putida
Length: 63 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMPIAQIHILEGRSDEQKETLIREVSEAISRSLDAPLTSVRVIITEMAKGHFGIGGELASKVRR
UniProtKB AC: Q01468 (positions: 2-58)
Coverage: 90%
Name: 2-hydroxymuconate tautomerase
Source organism: Pseudomonas putida
Length: 63 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMPIAQIHILEGRSDEQKETLIREVSEAISRSLDAPLTSVRVIITEMAKGHFGIGGELASKVRR
UniProtKB AC: Q01468 (positions: 2-57)
Coverage: 88%
Name: 2-hydroxymuconate tautomerase
Source organism: Pseudomonas putida
Length: 63 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMPIAQIHILEGRSDEQKETLIREVSEAISRSLDAPLTSVRVIITEMAKGHFGIGGELASKVRR
UniProtKB AC: Q01468 (positions: 2-58)
Coverage: 90%
Name: 2-hydroxymuconate tautomerase
Source organism: Pseudomonas putida
Length: 63 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMPIAQIHILEGRSDEQKETLIREVSEAISRSLDAPLTSVRVIITEMAKGHFGIGGELASKVRR
UniProtKB AC: Q01468 (positions: 2-58)
Coverage: 90%
Name: 2-hydroxymuconate tautomerase
Source organism: Pseudomonas putida
Length: 63 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMPIAQIHILEGRSDEQKETLIREVSEAISRSLDAPLTSVRVIITEMAKGHFGIGGELASKVRR
UniProtKB AC: Q01468 (positions: 2-58)
Coverage: 90%
Name: 2-hydroxymuconate tautomerase
Source organism: Pseudomonas putida
Length: 63 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMPIAQIHILEGRSDEQKETLIREVSEAISRSLDAPLTSVRVIITEMAKGHFGIGGELASKVRR
UniProtKB AC: Q01468 (positions: 2-58)
Coverage: 90%
Evidence demonstrating that the participating proteins are unstructured prior to the interaction and their folding is coupled to binding. Representative domain in related structures: -
Evidence level: Direct evidence
Evidence coverage: The full structure participates in mutual synergistic folding.
Complex Evidence:
4-oxalocrotonate tautomerase hexamer from Pseudomonas putida was shown by DSC to follow a two-state folding with the hexameric, dimeric and secondary structure all melting at the same temperature (PMID:20465238).
Chain A:
N/A
Chain B:
N/A
Chain C:
N/A
Chain D:
N/A
Chain E:
N/A
Chain F:
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). No related structure was found in the MFIB database.
Download the CIF file (.cif)
Download this entry's XML file (.xml)
Download this entry's JSON file (.json)
