5DO8: 1.8 Angstrom Crystal Structure Of Listeria Monocytogenes Lmo0184 Alpha-1,6-glucosidase

Citation:
Abstract
Here we employ a 'systems structural biology' approach to functionally characterize an unconventional alpha-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.
PDB ID: 5DO8Download
MMDB ID: 133167
PDB Deposition Date: 2015/9/10
Updated in MMDB: 2016/11
Experimental Method:
x-ray diffraction
Resolution: 1.8  Å
Source Organism:
Similar Structures:
Biological Unit for 5DO8: trimeric; determined by author
Molecular Components in 5DO8
Label Count Molecule
Proteins (3 molecules)
3
Lmo0184 Protein
Molecule annotation
Chemicals (10 molecules)
1
3
2
4
3
3
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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