Structure of the Yersinia pestis tip protein LcrV refined to 1.65 A resolution

View/ Open
Issue Date
2013-05-01Author
Chaudhury, Sukanya
Battaile, Kevin P.
Lovell, Scott
Plano, Gregory V.
De Guzman, Roberto N.
Publisher
International Union of Crystallography
Type
Article
Article Version
Scholarly/refereed, publisher version
Metadata
Show full item recordAbstract
The human pathogen Yersinia pestis requires the assembly of the type III secretion system (T3SS) for virulence. The structural component of the T3SS contains an external needle and a tip complex, which is formed by LcrV in Y. pestis. The structure of an LcrV triple mutant (K40A/D41A/K42A) in a C273S background has previously been reported to 2.2 Å resolution. Here, the crystal structure of LcrV without the triple mutation in a C273S background is reported at a higher resolution of 1.65 Å. Overall the two structures are similar, but there are also notable differences, particularly near the site of the triple mutation. The refined structure revealed a slight shift in the backbone positions of residues Gly28-Asn43 and displayed electron density in the loop region consisting of residues Ile46-Val63, which was disordered in the original structure. In addition, the helical turn region spanning residues Tyr77-Gln95 adopts a different orientation.
Description
This is the publisher's version, also available electronically from http://scripts.iucr.org/cgi-bin/paper?S1744309113008579.
ISSN
1744-3091Collections
Citation
Chaudhury, S.; Battaile, K. P.; Lovell, S.; Plano, G. V.; De Guzman, Roberto N. (2013). "Structure of the Yersinia pestis tip protein LcrV refined to 1.65 A resolution." Acta Crystallographica Section F., F69:477-481. http://www.dx.doi.org/10.1107/S1744309113008579.
Items in KU ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.
We want to hear from you! Please share your stories about how Open Access to this item benefits YOU.