6PTM
Crystal structure of apo exo-carrageenase GH42 from Bacteroides ovatus
Summary for 6PTM
Entry DOI | 10.2210/pdb6ptm/pdb |
Descriptor | Uncharacterized protein, 1,2-ETHANEDIOL (3 entities in total) |
Functional Keywords | exo-carrageenase, hydrolase |
Biological source | Bacteroides ovatus CL02T12C04 |
Total number of polymer chains | 1 |
Total formula weight | 88902.95 |
Authors | Hettle, A.G.,Boraston, A.B. (deposition date: 2019-07-16, release date: 2019-09-25, Last modification date: 2024-03-13) |
Primary citation | Hettle, A.G.,Hobbs, J.K.,Pluvinage, B.,Vickers, C.,Abe, K.T.,Salama-Alber, O.,McGuire, B.E.,Hehemann, J.H.,Hui, J.P.M.,Berrue, F.,Banskota, A.,Zhang, J.,Bottos, E.M.,Van Hamme, J.,Boraston, A.B. Insights into the kappa / iota-carrageenan metabolism pathway of some marinePseudoalteromonasspecies. Commun Biol, 2:474-474, 2019 Cited by PubMed Abstract: is a globally distributed marine-associated genus that can be found in a broad range of aquatic environments, including in association with macroalgal surfaces where they may take advantage of these rich sources of polysaccharides. The metabolic systems that confer the ability to metabolize this abundant form of photosynthetically fixed carbon, however, are not yet fully understood. Through genomics, transcriptomics, microbiology, and specific structure-function studies of pathway components we address the capacity of newly isolated marine pseudoalteromonads to metabolize the red algal galactan carrageenan. The results reveal that the κ/ι-carrageenan specific polysaccharide utilization locus (CarPUL) enables isolates possessing this locus the ability to grow on this substrate. Biochemical and structural analysis of the enzymatic components of the CarPUL promoted the development of a detailed model of the κ/ι-carrageenan metabolic pathway deployed by pseudoalteromonads, thus furthering our understanding of how these microbes have adapted to a unique environmental niche. PubMed: 31886414DOI: 10.1038/s42003-019-0721-y PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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