4JBU

1.65A structure of the T3SS tip protein LcrV (G28-D322, C273S) from Yersinia pestis

Summary for 4JBU

• Entry DOI: 10.2210/pdb4jbu/pdb
• Descriptor: Virulence-associated V antigen, TETRAETHYLENE GLYCOL (3 entities in total)
• Functional Keywords: lcrv, t3ss, tip protein, yersinia pestis, protein binding
• Biological source: Yersinia pestis
• Cellular location: Secreted: P0C7U7
• Total number of polymer chains: 1
• Total formula weight: 34153.53

Authors

Lovell, S.,Chaudhury, S.,Battaile, K.P.,Plano, G.,De Guzman, R.N. (deposition date: 2013-02-20, release date: 2013-05-08, Last modification date: 2023-09-20)

Primary citation

Chaudhury, S.,Battaile, K.P.,Lovell, S.,Plano, G.V.,De Guzman, R.N.
Structure of the Yersinia pestis tip protein LcrV refined to 1.65A resolution
Acta Crystallogr.,Sect.F, 69:477-481, 2013

PubMed 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.

PubMed: 23695558
DOI: 10.1107/S1744309113008579

Experimental method

X-RAY DIFFRACTION (1.65 Å)