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5F7U

Cycloalternan-forming enzyme from Listeria monocytogenes in complex with pentasaccharide substrate

Summary for 5F7U
Entry DOI10.2210/pdb5f7u/pdb
Related PRD IDPRD_900001
DescriptorCycloalternan-forming enzyme, alpha-D-glucopyranose-(1-6)-alpha-D-glucopyranose-(1-3)-[alpha-D-glucopyranose-(1-6)]alpha-D-glucopyranose, alpha-D-glucopyranose-(1-6)-alpha-D-glucopyranose, ... (7 entities in total)
Functional Keywordscomplex, structural genomics, center for structural genomics of infectious diseases, csgid, sugar binding protein
Biological sourceListeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Total number of polymer chains1
Total formula weight120913.24
Authors
Light, S.H.,Anderson, W.F.,Center for Structural Genomics of Infectious Diseases (CSGID) (deposition date: 2015-12-08, release date: 2016-09-21, 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 (1.7 Å)
Structure validation

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数据于2025-06-18公开中

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