Description
Experimental Technique/Method:X-RAY DIFFRACTION
Resolution:1.95
Classification:STRUCTURAL GENOMICS, UNKNOWN FUNCTION
Release Date:2012-11-21
Deposition Date:2012-11-06
Revision Date:2014-04-23#2017-11-15
Molecular Weight:34728.95
Macromolecule Type:Protein
Residue Count:316
Atom Site Count:1972
DOI:10.2210/pdb4hvn/pdb
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.
Resolution:1.95
Classification:STRUCTURAL GENOMICS, UNKNOWN FUNCTION
Release Date:2012-11-21
Deposition Date:2012-11-06
Revision Date:2014-04-23#2017-11-15
Molecular Weight:34728.95
Macromolecule Type:Protein
Residue Count:316
Atom Site Count:1972
DOI:10.2210/pdb4hvn/pdb
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.
| Date made available | 2012 |
|---|---|
| Publisher | RCSB-PDB |