A functional role of Rv1738 in Mycobacterium tuberculosis persistence suggested by racemic protein crystallography
- Univ. of Auckland, Auckland (New Zealand)
- Univ. of Chicago, Chicago, IL (United States)
Racemic protein crystallography was used to determine the X-ray structure of the predicted Mycobacterium tuberculosis protein Rv1738, which had been completely recalcitrant to crystallization in its natural L-form. Native chemical ligation was used to synthesize both L-protein and D-protein enantiomers of Rv1738. Crystallization of the racemic {D-protein + L-protein} mixture was immediately successful. The resulting crystals diffracted to high resolution and also enabled facile structure determination because of the quantized phases of the data from centrosymmetric crystals. The X-ray structure of Rv1738 revealed striking similarity with bacterial hibernation factors, despite minimal sequence similarity. As a result, we predict that Rv1738, which is highly up-regulated in conditions that mimic the onset of persistence, helps trigger dormancy by association with the bacterial ribosome.
- Research Organization:
- Argonne National Laboratory (ANL), Argonne, IL (United States)
- Sponsoring Organization:
- USDOE
- Grant/Contract Number:
- AC02-06CH11357
- OSTI ID:
- 1178127
- Journal Information:
- Proceedings of the National Academy of Sciences of the United States of America, Vol. 112, Issue 14; ISSN 0027-8424
- Publisher:
- National Academy of Sciences, Washington, DC (United States)Copyright Statement
- Country of Publication:
- United States
- Language:
- English
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