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4HVN

Crystal structure of hypothetical protein with ketosteroid isomerase-like protein fold from Catenulispora acidiphila DSM 44928 in complex with Trimethylamine.

Summary for 4HVN
Entry DOI10.2210/pdb4hvn/pdb
Related4H3U
Descriptorhypothetical protein, N,N-dimethylmethanamine (3 entities in total)
Functional Keywordsstructural genomics, psi-biology, midwest center for structural genomics, mcsg, unknown function
Biological sourceCatenulispora acidiphila
Total number of polymer chains2
Total formula weight34728.95
Authors
Filippova, E.V.,Minasov, G.,Shuvalova, L.,Kiryukhina, O.,Jedrzejczak, R.,Joachimiak, A.,Anderson, W.F.,Midwest Center for Structural Genomics (MCSG) (deposition date: 2012-11-06, release date: 2012-11-21, Last modification date: 2024-11-06)
Primary citationFilippova, E.V.,Luan, C.H.,Dunne, S.F.,Kiryukhina, O.,Minasov, G.,Shuvalova, L.,Anderson, W.F.
Structural characterization of a hypothetical protein: a potential agent involved in trimethylamine metabolism in Catenulispora acidiphila.
J.Struct.Funct.Genom., 15:33-40, 2014
Cited by
PubMed Abstract: Catenulispora acidiphila is a newly identified lineage of actinomycetes that produces antimicrobial activities and represents a promising source of novel antibiotics and secondary metabolites. Among the discovered protein coding genes, 68 % were assigned a putative function, while the remaining 32 % are genes encoding "hypothetical" proteins. Caci_0382 is one of the "hypothetical" proteins that has very few homologs. Sequence analysis shows that the protein belongs to the NTF2-like protein family. The structure of Caci_0382 demonstrates that it shares the same fold and has a similar active site as limonene-1,2-epoxide hydrolase, which suggests that it may have a related function. Using a fluorescence thermal shift assay, we identified stabilizing compounds that suggest potential natural ligands of Caci_0382. Using this information, we determined the crystal structure in complex with trimethylamine to provide a better understanding of the function of this uncharacterized protein.
PubMed: 24562475
DOI: 10.1007/s10969-014-9176-z
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.95 Å)
Structure validation

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