4phb

Structure of the polysaccharide lyase-like protein Cthe_2159 from C. thermocellum, Gadolinium derivative

spinqualitylabelsall models 4phb, resolution 2.18Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4phb is a 1 chain structure with sequence from Acetivibrio thermocellus ATCC 27405. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.1781Å Ligands: GD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CBDP_ACET2 Binds cellulosic and pectic substrates. Displays no enzyme activity (in vitro). Publication Abstract from PubMed Microorganisms that degrade biomass produce diverse assortments of carbohydrate-active enzymes and binding modules. Despite tremendous advances in the genomic sequencing of these organisms, many genes do not have an ascribed function owing to low sequence identity to genes that have been annotated. Consequently, biochemical and structural characterization of genes with unknown function is required to complement the rapidly growing pool of genomic sequencing data. A protein with previously unknown function (Cthe_2159) was recently isolated in a genome-wide screen using phage display to identify cellulose-binding protein domains from the biomass-degrading bacterium Clostridium thermocellum. Here, the crystal structure of Cthe_2159 is presented and it is shown that it is a unique right-handed parallel beta-helix protein. Despite very low sequence identity to known beta-helix or carbohydrate-active proteins, Cthe_2159 displays structural features that are very similar to those of polysaccharide lyase (PL) families 1, 3, 6 and 9. Cthe_2159 is conserved across bacteria and some archaea and is a member of the domain of unknown function family DUF4353. This suggests that Cthe_2159 is the first representative of a previously unknown family of cellulose and/or acid-sugar binding beta-helix proteins that share structural similarities with PLs. Importantly, these results demonstrate how functional annotation by biochemical and structural analysis remains a critical tool in the characterization of new gene products. A new family of beta-helix proteins with similarities to the polysaccharide lyases.,Close DW, D'Angelo S, Bradbury AR Acta Crystallogr D Biol Crystallogr. 2014 Oct 1;70(Pt 10):2583-92. doi:, 10.1107/S1399004714015934. Epub 2014 Sep 27. PMID:25286843 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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