Database accession: MF7000233
Name: DR2232 (E46A mutant)
PDB ID: 5hwu
Experimental method: X-ray (2.10 Å)
Assembly: Homodimer
Source organism: Deinococcus radiodurans
Primary publication of the structure:
Mota CS, Gonçalves AM, de Sanctis D
Deinococcus radiodurans DR2231 is a two-metal-ion mechanism hydrolase with exclusive activity on dUTP.
(2016) FEBS J. 283: 4274-4290
PMID: 27739259
Abstract:
Not available.
Annotations from the GeneOntology database. Only terms that fit at least two of the interacting proteins are shown. Molecular function:
metal ion binding metal ion binding
nucleoside triphosphate diphosphatase activity nucleoside triphosphate diphosphatase activity
Biological process: not assigned
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: HAD superfamily Cof-like phosphohydrolase
Source organism: Deinococcus radiodurans
Length: 148 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMSDLPCPPTNAERLHEFHRAIGAATPERPTPPPPELLRLRQTLLDEESAEVRAEIDHLLARQAAGEALSAGDLAPLAHELADLLYVTYGALDQLGIDADAVFAEVHRANLSKASGPRRADGKQLKPEGWRPADVRGVIERLQHAPADD
UniProtKB AC: Q9RS96 (positions: 7-144)
Coverage: 93%
Name: HAD superfamily Cof-like phosphohydrolase
Source organism: Deinococcus radiodurans
Length: 148 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMSDLPCPPTNAERLHEFHRAIGAATPERPTPPPPELLRLRQTLLDEESAEVRAEIDHLLARQAAGEALSAGDLAPLAHELADLLYVTYGALDQLGIDADAVFAEVHRANLSKASGPRRADGKQLKPEGWRPADVRGVIERLQHAPADD
UniProtKB AC: Q9RS96 (positions: 7-144)
Coverage: 93%
Evidence demonstrating that the participating proteins are unstructured prior to the interaction and their folding is coupled to binding. Representative domain in related structures: Phosphoribosyl-ATP pyrophosphohydrolase
Evidence level: Direct evidence
Evidence coverage: The full structure participates in mutual synergistic folding.
Complex Evidence:
Phosphoribosyl-ATP pyrophosphohydrolases show a very unusual interlaced segment-swapped dimer, which implies that this obligatory dimer assembly is important for their function. Size-exclusion chromatography combined with static light scattering confirmed that the dimer is the major oligomeric state in solution (PMID:20944217). Upon dimer formation, DR2231 helices 2 and 3 from one monomer stack antiparallel to helices 2′ and 3′ of the other monomer, respectively. A stable four-helix bundle is formed in the center. The intertwining of the two hairpin structures produces an extensive subunit-subunit interface (PMID:21733847).
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)
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