4H3U

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

Summary for 4H3U

• Entry DOI: 10.2210/pdb4h3u/pdb
• Descriptor: hypothetical protein, CADMIUM ION, CHLORIDE ION, ... (5 entities in total)
• Functional Keywords: structural genomics, psi-biology, midwest center for structural genomics, mcsg, unknown function
• Biological source: Catenulispora acidiphila
• Total number of polymer chains: 2
• Total formula weight: 35763.74

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: 2012-09-14, release date: 2012-10-03, Last modification date: 2017-11-15)

Primary citation

Filippova, 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

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

Experimental method

X-RAY DIFFRACTION (1.15 Å)