4hvn | pdb_00004hvn

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

spinqualitylabelsall models 4hvn, resolution 1.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4hvn is a 2 chain structure with sequence from Catenulispora acidiphila DSM 44928. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: KEN, MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function C7PVH9_CATAD Publication Abstract from PubMed 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. Structural characterization of a hypothetical protein: a potential agent involved in trimethylamine metabolism in Catenulispora acidiphila.,Filippova EV, Luan CH, Dunne SF, Kiryukhina O, Minasov G, Shuvalova L, Anderson WF J Struct Funct Genomics. 2014 Mar;15(1):33-40. doi: 10.1007/s10969-014-9176-z., Epub 2014 Feb 22. PMID:24562475 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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