Database accession: MF7000825
Name: Mouse mRNA decapping enzyme (DcpS)
PDB ID: 1vlr
Experimental method: X-ray (1.83 Å)
Assembly: Homodimer
Source organism: Mus musculus
Primary publication of the structure:
Han GW, Schwarzenbacher R, McMullan D, Abdubek P, Ambing E, Axelrod H, Biorac T, Canaves JM, Chiu HJ, Dai X, Deacon AM, DiDonato M, Elsliger MA, Godzik A, Grittini C, Grzechnik SK, Hale J, Hampton E, Haugen J, Hornsby M, Jaroszewski L, Klock HE, Koesema E, Kreusch A, Kuhn P, Lesley SA, McPhillips TM, Miller MD, Moy K, Nigoghossian E, Paulsen J, Quijano K, Reyes R, Spraggon G, Stevens RC, van den Bedem H, Velasquez J, Vincent J, White A, Wolf G, Xu Q, Hodgson KO, Wooley J, Wilson IA
Crystal structure of an Apo mRNA decapping enzyme (DcpS) from Mouse at 1.83 A resolution.
(2005) Proteins 60: 797-802
PMID: 16001405
Abstract:
Not available.
Annotations from the GeneOntology database. Only terms that fit at least two of the interacting proteins are shown. Molecular function:
5'-(N(7)-methyl 5'-triphosphoguanosine)-[mRNA] diphosphatase activity 5'-(N(7)-methyl 5'-triphosphoguanosine)-[mRNA] diphosphatase activity
identical protein binding identical protein binding
RNA 7-methylguanosine cap binding RNA 7-methylguanosine cap binding
Biological process:
deadenylation-dependent decapping of nuclear-transcribed mRNA deadenylation-dependent decapping of nuclear-transcribed mRNA
mRNA cis splicing, via spliceosome mRNA cis splicing, via spliceosome
Cellular component:
cytoplasm cytoplasm
cytosol cytosol
mitochondrion mitochondrion
nucleoplasm nucleoplasm
nucleus nucleus
P-body P-body
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: m7GpppX diphosphatase
Source organism: Mus musculus
Length: 338 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMADTAPQLKRKREQEAEEAETPSTEEKEAGVGNGTSAPVRLPFSGFRVQKVLRESARDKIIFLHGKVNEDSGDTHGEDAVVILEKTPFQVEHVAQLLTGSPELKLQFSNDIYSTYNLFPPRHLSDIKTTVVYPATEKHLQKYMRQDLRLIRETGDDYRTITLPYLESQSLSIQWVYNILDKKAEADRIVFENPDPSDGFVLIPDLKWNQQQLDDLYLIAICHRRGIRSLRDLTPEHLPLLRNILREGQEAILKRYQVTGDRLRVYLHYLPSYYHLHVHFTALGFEAPGSGVERAHLLAQVIENLECDPKHYQQRTLTFALRTDDPLLQLLQKAQQERN
UniProtKB AC: Q9DAR7 (positions: 38-337)
Coverage: 88%
Name: m7GpppX diphosphatase
Source organism: Mus musculus
Length: 338 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMADTAPQLKRKREQEAEEAETPSTEEKEAGVGNGTSAPVRLPFSGFRVQKVLRESARDKIIFLHGKVNEDSGDTHGEDAVVILEKTPFQVEHVAQLLTGSPELKLQFSNDIYSTYNLFPPRHLSDIKTTVVYPATEKHLQKYMRQDLRLIRETGDDYRTITLPYLESQSLSIQWVYNILDKKAEADRIVFENPDPSDGFVLIPDLKWNQQQLDDLYLIAICHRRGIRSLRDLTPEHLPLLRNILREGQEAILKRYQVTGDRLRVYLHYLPSYYHLHVHFTALGFEAPGSGVERAHLLAQVIENLECDPKHYQQRTLTFALRTDDPLLQLLQKAQQERN
UniProtKB AC: Q9DAR7 (positions: 39-337)
Coverage: 88%
Evidence demonstrating that the participating proteins are unstructured prior to the interaction and their folding is coupled to binding. Representative domain in related structures: Scavenger mRNA decapping enzyme (DcpS)
Evidence level: Indirect evidence
Evidence coverage: Only some parts of the structure participates in mutual synergistic folding.
Complex Evidence:
Multidomain structure, where the domain-swapped N-terminal domain is responsible for dimerization. The extensive interface, symmetry, topology, beta sheet augmentation and buried surface area suggest that the N-terminal dimerization domain behaves as a single rigid domain and the monomers would not be stable on their own. Gel-filtration chromatography also suggested a dimeric form (PMID:15068804).
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)
Download this entry's JSON file (.json)
