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5DO8

1.8 Angstrom crystal structure of Listeria monocytogenes Lmo0184 alpha-1,6-glucosidase

Summary for 5DO8
Entry DOI10.2210/pdb5do8/pdb
DescriptorLmo0184 protein, beta-D-glucopyranose, CHLORIDE ION, ... (5 entities in total)
Functional Keywordsglycoside hydrolase family 13, structural genomics, center for structural genomics of infectious diseases, csgid, hydrolase
Biological sourceListeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Total number of polymer chains3
Total formula weight197322.36
Authors
Light, S.H.,Halavaty, A.S.,Anderson, W.F.,Center for Structural Genomics of Infectious Diseases (CSGID) (deposition date: 2015-09-10, release date: 2015-09-30, Last modification date: 2023-09-27)
Primary citationLight, S.H.,Cahoon, L.A.,Halavaty, A.S.,Freitag, N.E.,Anderson, W.F.
Structure to function of an alpha-glucan metabolic pathway that promotes Listeria monocytogenes pathogenesis.
Nat Microbiol, 2:16202-16202, 2016
Cited by
PubMed Abstract: Here we employ a 'systems structural biology' approach to functionally characterize an unconventional α-glucan metabolic pathway from the food-borne pathogen Listeria monocytogenes (Lm). Crystal structure determination coupled with basic biochemical and biophysical assays allowed for the identification of anabolic, transport, catabolic and regulatory portions of the cycloalternan pathway. These findings provide numerous insights into cycloalternan pathway function and reveal the mechanism of repressor, open reading frame, kinase (ROK) transcription regulators. Moreover, by developing a structural overview we were able to anticipate the cycloalternan pathway's role in the metabolism of partially hydrolysed starch derivatives and demonstrate its involvement in Lm pathogenesis. These findings suggest that the cycloalternan pathway plays a role in interspecies resource competition-potentially within the host gastrointestinal tract-and establish the methodological framework for characterizing bacterial systems of unknown function.
PubMed: 27819654
DOI: 10.1038/nmicrobiol.2016.202
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.8 Å)
Structure validation

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