The crystal structure of a hypothetical protein, TM1457, from Thermotoga maritima has been determined at 2.0 Å resolution. TM1457 belongs to the DUF464 family (57 members) for which there is no known function. The structure shows that it is composed of two helices in contact with one side of a five-stranded β-sheet. Two identical monomers form a pseudo-dimer in the asymmetric unit. There is a large cleft between the first α-helix and the second β-strand. This cleft may be functionally important, since the two highly conserved motifs, GHA and VCAXV(S/T), are located around the cleft. A structural comparison of TM1457 with known protein structures shows the best hit with another hypothetical protein, Ybl001C from Saccharomyces cerevisiae, though they share low structural similarity. Therefore, TM1457 still retains a unique topology and reveals a novel fold.
Bibliographical noteFunding Information:
We are grateful to Barbara Gold for cloning, Marlene Henriquez, and Bruno Martinez for expression studies and cell paste preparation, and John-Marc Chandonia for bioinformatics search of the gene. We also are grateful to the staff at the Advanced Light Source which is supported by the Director, Office of Science, Office of Basic Energy Sciences, Materials Sciences Division, of the US Department of Energy under Contract No. DE-AC03-76SF00098 at Lawrence Berkeley National Laboratory. The work described here was supported by the National Institutes of Health GM 62412.
- Crystal structure
- Gi 4982022
- Hypothetical protein