Crystal Structure of the Protease-Resistant Core Domain of Yersinia Pestis Virulence Factor Yopr

Journal Article · Sat Jan 01 04:00:00 EST 2005 · Protein Sci.

DOI:https://doi.org/10.1110/ps.051446405· OSTI ID:913752

Schubot, F; Cherry, S; Austin, B; Tropea, J; Waugh, D

Yersinia pestis, the causative agent of the plague, employs a type III secretion system (T3SS) to secrete and translocate virulence factors into the cytoplasm of mammalian host cells. One of the secreted virulence factors is YopR. Little is known about the function of YopR other than that it is secreted into the extracellular milieu during the early stages of infection and that it contributes to virulence. Hoping to gain some insight into the function of YopR, we determined the crystal structure of its protease-resistant core domain, which consists of residues 38--149 out of 165 amino acids. The core domain is composed of five {alpha}-helices that display unexpected structural similarity with one domain of YopN, a central regulator of type III secretion in Y. pestis. This finding raises the possibility that YopR may play a role in the regulation of type III secretion.

• Research Organization: Brookhaven National Laboratory (BNL) National Synchrotron Light Source
• Sponsoring Organization: Doe - Office Of Science
• DOE Contract Number: AC02-98CH10886
• OSTI ID: 913752
• Report Number(s): BNL--78320-2007-JA
• Journal Information: Protein Sci., Journal Name: Protein Sci. Vol. 14
• Country of Publication: United States
• Language: English

Related Subjects

36 MATERIALS SCIENCE
AMINO ACIDS
CRYSTAL STRUCTURE
CYTOPLASM
REGULATIONS
RESIDUES
SECRETION
VIRULENCE
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