General Information

Database accession: MF7000201

Name: UPF0066 protein AF0241

PDB ID: 2nv4 PDBe

Experimental method: X-ray (2.20 Å)

Assembly: Homodimer

Source organism: Archaeoglobus fulgidus

Primary publication of the structure:

Forouhar F, Kuzin A, Seetharaman J, Lee I, Zhou W, Abashidze M, Chen Y, Yong W, Janjua H, Fang Y, Wang D, Cunningham K, Xiao R, Acton TB, Pichersky E, Klessig DF, Porter CW, Montelione GT, Tong L
Functional insights from structural genomics.

(2007) J. Struct. Funct. Genomics 8: 37-44

PMID: 17588214 PubMed

Abstract:

Structural genomics efforts have produced structural information, either directly or by modeling, for thousands of proteins over the past few years. While many of these proteins have known functions, a large percentage of them have not been characterized at the functional level. The structural information has provided valuable functional insights on some of these proteins, through careful structural analyses, serendipity, and structure-guided functional screening. Some of the success stories based on structures solved at the Northeast Structural Genomics Consortium (NESG) are reported here. These include a novel methyl salicylate esterase with important role in plant innate immunity, a novel RNA methyltransferase (H. influenzae yggJ (HI0303)), a novel spermidine/spermine N-acetyltransferase (B. subtilis PaiA), a novel methyltransferase or AdoMet binding protein (A. fulgidus AF_0241), an ATP:cob(I)alamin adenosyltransferase (B. subtilis YvqK), a novel carboxysome pore (E. coli EutN), a proline racemase homolog with a disrupted active site (B. melitensis BME11586), an FMN-dependent enzyme (S. pneumoniae SP_1951), and a 12-stranded beta-barrel with a novel fold (V. parahaemolyticus VPA1032).


Function and Biology Annotations from the GeneOntology database. Only terms that fit at least two of the interacting proteins are shown.

Molecular function:

tRNA (L-threonylcarbamoyladenosine(37)-C2) methyltransferase activity tRNA (L-threonylcarbamoyladenosine(37)-C2) methyltransferase activity GeneOntology

Biological process: not assigned

Cellular component: not assigned

Structure Summary 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


Chain A

Name: S-adenosyl-L-methionine-binding protein AF_0241

Source organism: Archaeoglobus fulgidus

Length: 139 residues

Sequence:Sequence according to the corresponding UniProt protein segmentMILKPIGVVKSPFKTQNDAPRQGRFSDAVSEIAIFDEYADGLHKIENLRHIIVLYWMDKASRDKLRVVPPGETEERGVFTTRSPSRPNPIGLCVVEILEVERNRLKVRWLDALDGSPVIDIKKYSPEIDCVNQLEGQQP

UniProtKB AC: O29998 (positions: 1-133) UniProt

Coverage: 95%

Chain B

Name: S-adenosyl-L-methionine-binding protein AF_0241

Source organism: Archaeoglobus fulgidus

Length: 139 residues

Sequence:Sequence according to the corresponding UniProt protein segmentMILKPIGVVKSPFKTQNDAPRQGRFSDAVSEIAIFDEYADGLHKIENLRHIIVLYWMDKASRDKLRVVPPGETEERGVFTTRSPSRPNPIGLCVVEILEVERNRLKVRWLDALDGSPVIDIKKYSPEIDCVNQLEGQQP

UniProtKB AC: O29998 (positions: 1-133) UniProt

Coverage: 95%

Evidence 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: Insufficient evidence (candidate)

Evidence coverage: The full structure participates in mutual synergistic folding.

Complex Evidence:

There is no information on the stability/disorder of the monomeric forms. AF_0241 is a dimer, both in solution and in the crystal (PMID:17588214).

Chain A:

N/A

Chain B:

N/A

Surface and contacts features:

Related Structure(s) 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.


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