Abstract
The crystal structure of PA1994 from Pseudomonas aeruginosa, a member of the Pfam PF06475 family classified as a domain of unknown function (DUF1089), reveals a novel fold comprising a 15-stranded β-sheet wrapped around a single α-helix that assembles into a tight dimeric arrangement. The remote structural similarity to lipoprotein localization factors, in addition to the presence of an acidic pocket that is conserved in DUF1089 homologs, phospholipid-binding and sugar-binding proteins, indicate a role for PA1994 and the DUF1089 family in glycolipid metabolism. Genome-context analysis lends further support to the involvement of this family of proteins in glycolipid metabolism and indicates possible activation of DUF1089 homologs under conditions of bacterial cell-wall stress or host-pathogen interactions.
Highlights
IntroductionIn an effort to extend the structural coverage of proteins for which the biological function is unknown and cannot be deduced by homology (i.e. domains of unknown function; DUFs), targets were selected from Pfam protein family PF06745 (DUF1089)
In an effort to extend the structural coverage of proteins for which the biological function is unknown and cannot be deduced by homology, targets were selected from Pfam protein family PF06745 (DUF1089)
We show that global and local structural and chemical similarities to lipid-binding proteins suggest the involvement of PA1994 with the bacterial membrane, while genome-context analysis supports a role for the DUF1089 family in glycolipid metabolism that is likely to be triggered under conditions of osmotic stress or host–pathogen interactions
Summary
In an effort to extend the structural coverage of proteins for which the biological function is unknown and cannot be deduced by homology (i.e. domains of unknown function; DUFs), targets were selected from Pfam protein family PF06745 (DUF1089). We show that global and local structural and chemical similarities to lipid-binding proteins suggest the involvement of PA1994 with the bacterial membrane, while genome-context analysis supports a role for the DUF1089 family in glycolipid metabolism that is likely to be triggered under conditions of osmotic stress or host–pathogen interactions. These structural insights should help to guide future functional studies
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