Abstract
The crystal structure of Jann_2411 from Jannaschia sp. strain CCS1, a member ofthe Pfam PF07336 family classified as a domain of unknown function (DUF1470), was solved to a resolution of 1.45 Å by multiple-wavelength anomalous dispersion (MAD). This protein is the first structural representative of the DUF1470 Pfam family. Structural analysis revealed a two-domain organization, with the N-terminal domain presenting a new fold called the ABATE domain that may bind an as yet unknown ligand. The C-terminal domain forms a treble-clef zinc finger that is likely to be involved in DNA binding. Analysis of the Jann_2411 protein and the broader ABATE-domain family suggests a role as stress-induced transcriptional regulators.
Highlights
The complete genome sequences of hundreds of organisms are known, each of which contains thousands of genes that have evolved to create the bewildering diversity of life
Structural analysis revealed a two-domain organization, with the Nterminal domain consisting of a new fold that we call the ABATE domain and the C-terminal domain forming a treble-clef zinc finger that we have termed the CGNR zinc-finger domain after a characteristic sequence motif that is conserved in this family
Jan_2411 forms a dimer, with both monomers implicated in the formation of a putative DNA binding site, and analysis of its genomic context suggests a role for the ABATE-domain family in stress-induced transcriptional regulation
Summary
The complete genome sequences of hundreds of organisms are known, each of which contains thousands of genes that have evolved to create the bewildering diversity of life. To understand this complexity at the molecular level requires the investigation of the function and structure of a vast number of proteins. The Pfam database (Finn et al, 2008) contains over 2000 such families, termed domains of unknown function (DUFs), and understanding their structure will help to elucidate their function. To extend the structural coverage of proteins with uncharacterized biological function, we targeted the Pfam protein family DUF1470 and have determined the structure of the Jann_2411 gene product from Jannaschia sp. Jan_2411 forms a dimer, with both monomers implicated in the formation of a putative DNA binding site, and analysis of its genomic context suggests a role for the ABATE-domain family in stress-induced transcriptional regulation
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