5htf | pdb_00005htf
Crystal Structure of PrsA1 from Listeria monocytogenes
Structural highlights
FunctionPRSA1_LISMO Plays a major role in protein secretion by helping the post-translocational extracellular folding of several secreted proteins. Publication Abstract from PubMedListeria monocytogenes is a Gram-positive environmental bacterium that lives within soil but transitions into a pathogen upon contact with a mammalian host. The transition of L. monocytogenes from soil dweller to cytosolic pathogen is dependent upon secreted virulence factors that mediate cell invasion and intracellular growth. PrsA1 and PrsA2 are secreted bacterial lipoprotein chaperones that contribute to the folding of proteins translocated across the bacterial membrane; PrsA2 is required for L. monocytogenes virulence, whereas the function of PrsA1 remains to be determined. We have solved an X-ray crystal structure of PrsA1 and have used this model to guide comparison structure-based mutagenesis studies with PrsA2. Targeted mutagenesis of PrsA2 demonstrates that oligomerization of PrsA2 as well as molecular features of the foldase domain are required for protein secretion and virulence, whereas a functional role was uncovered for PrsA1 in bacterial resistance to alcohol. Interestingly, PrsA2 membrane localization is not required for all PrsA2-dependent activities, suggesting that the lipoprotein retains function when released from the bacterial cell. PrsA chaperones are thus multifaceted proteins with distinct domains adapted to accommodate the functional needs of a diverse array of secreted substrates. This article is protected by copyright. All rights reserved. A structural comparison of Listeria monocytogenes protein chaperones PrsA1 and PrsA2 reveals molecular features required for virulence.,Cahoon LA, Freitag NE, Prehna G Mol Microbiol. 2016 Mar 23. doi: 10.1111/mmi.13367. PMID:27007641[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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