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Structure of the Yersinia pestis tip protein LcrV refined to 1.65 A resolution
Chaudhury, Sukanya Battaile, Kevin P. Lovell, Scott Plano, Gregory V. De Guzman, Roberto N.
Chaudhury, Sukanya
Battaile, Kevin P.
Lovell, Scott
Plano, Gregory V.
De Guzman, Roberto N.
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Abstract
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.
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This is the publisher's version, also available electronically from http://scripts.iucr.org/cgi-bin/paper?S1744309113008579.
Date
2013-05-01
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International Union of Crystallography
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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.