Database accession: MF4110003
Name: 5-hydroxyisourate hydrolase (Danio rerio)
PDB ID: 2h1x
Experimental method: X-ray (1.98 Å)
Assembly: Homotetramer
Source organism: Danio rerio
Primary publication of the structure:
Zanotti G, Cendron L, Ramazzina I, Folli C, Percudani R, Berni R
Structure of zebra fish HIUase: insights into evolution of an enzyme to a hormone transporter.
(2006) J. Mol. Biol. 363: 1-9
PMID: 16952372
Abstract:
During early vertebrate evolution, a duplication event in the gene encoding 5-hydroxyisourate hydrolase (HIUase), a widely distributed enzyme of purine metabolism, gave rise to transthyretin (TTR), a thyroid hormone transporter. We report here on the crystal structure of zebra fish HIUase in two different crystal forms. Despite the phylogenetic distance, this structure compares well with those of newly characterized bacterial HIUases, especially with regard to catalytic regions, which are highly preserved. Comparison with TTR structure reveals a highly conserved scaffold, harbouring distinct functional sites located in the same regions of the two vertebrate proteins. Residues that are differentially conserved in HIUases compared to TTR map in putative catalytic regions occupying significant portions of the two halves of a central channel that transverses the whole TTR protein. The evolution of TTR has been accompanied by remarkable changes of the HIUase active sites that gave rise to a channel open at both ends, thus allowing free access to hormone molecules.
Annotations from the GeneOntology database. Only terms that fit at least two of the interacting proteins are shown. Molecular function:
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
hydroxyisourate hydrolase activity hydroxyisourate hydrolase activity
Biological process:
purine nucleobase metabolic process purine nucleobase metabolic process
urate catabolic process urate catabolic process
Cellular component:
peroxisome peroxisome
Structural annotations of the participating protein chains.Entry contents: 4 distinct polypeptide molecules
Chains: A, B, C, D
Notes: All chains according to the most probable oligomerization state stored in PDBe were considered.
Number of unique protein segments: 1
Name: 5-hydroxyisourate hydrolase
Source organism: Danio rerio
Length: 138 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMNRLQHIRGHIVSADKHINMSATLLSPLSTHVLNIAQGVPGANMTIVLHRLDPVSSAWNILTTGITNDDGRCPGLITKENFIAGVYKMRFETGKYWDALGETCFYPYVEIVFTITNTSQHYHVPLLLSRFSYSTYRGS
UniProtKB AC: Q06S87 (positions: 26-138)
Coverage: 81%
Name: 5-hydroxyisourate hydrolase
Source organism: Danio rerio
Length: 138 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMNRLQHIRGHIVSADKHINMSATLLSPLSTHVLNIAQGVPGANMTIVLHRLDPVSSAWNILTTGITNDDGRCPGLITKENFIAGVYKMRFETGKYWDALGETCFYPYVEIVFTITNTSQHYHVPLLLSRFSYSTYRGS
UniProtKB AC: Q06S87 (positions: 26-138)
Coverage: 81%
Name: 5-hydroxyisourate hydrolase
Source organism: Danio rerio
Length: 138 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMNRLQHIRGHIVSADKHINMSATLLSPLSTHVLNIAQGVPGANMTIVLHRLDPVSSAWNILTTGITNDDGRCPGLITKENFIAGVYKMRFETGKYWDALGETCFYPYVEIVFTITNTSQHYHVPLLLSRFSYSTYRGS
UniProtKB AC: Q06S87 (positions: 26-138)
Coverage: 81%
Name: 5-hydroxyisourate hydrolase
Source organism: Danio rerio
Length: 138 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMNRLQHIRGHIVSADKHINMSATLLSPLSTHVLNIAQGVPGANMTIVLHRLDPVSSAWNILTTGITNDDGRCPGLITKENFIAGVYKMRFETGKYWDALGETCFYPYVEIVFTITNTSQHYHVPLLLSRFSYSTYRGS
UniProtKB AC: Q06S87 (positions: 26-138)
Coverage: 81%
Evidence demonstrating that the participating proteins are unstructured prior to the interaction and their folding is coupled to binding. Representative domain in related structures: HIUase/Transthyretin family
Evidence level: Direct evidence
Evidence coverage: The full structure participates in mutual synergistic folding.
Complex Evidence:
The protein belongs to the 5-hydroxyisourate hydrolase (HIUase)/transthyretin protein family. Accordingly, the complex adopts a transthyterin-like fold (based on Pfam entry PF00576.18 and the publication PMID:16952372). Transthyretin was shown in calorimetrics experiments to follow two-state folding/binding kinetics with the emergence of structure being linked to oligomerization (PMID:11152276).
Chain A:
N/A
Chain B:
N/A
Chain C:
N/A
Chain D:
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)
Download this entry's JSON file (.json)
