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6PTM

Crystal structure of apo exo-carrageenase GH42 from Bacteroides ovatus

Summary for 6PTM
Entry DOI10.2210/pdb6ptm/pdb
DescriptorUncharacterized protein, 1,2-ETHANEDIOL (3 entities in total)
Functional Keywordsexo-carrageenase, hydrolase
Biological sourceBacteroides ovatus CL02T12C04
Total number of polymer chains1
Total formula weight88902.95
Authors
Hettle, A.G.,Boraston, A.B. (deposition date: 2019-07-16, release date: 2019-09-25, Last modification date: 2024-03-13)
Primary citationHettle, 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: 31886414
DOI: 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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数据于2024-11-06公开中

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