7la6

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THE STRUCTURE OF A SENSOR DOMAIN OF A HISTIDINE KINASE (VxrA) FROM VIBRIO CHOLERAE O1 BIOVAR ELTOR STR. N16961, N239 deletion mutant

Structural highlights

7la6 is a 1 chain structure with sequence from Vibrio cholerae O1 biovar El Tor str. N16961. This structure supersedes the now removed PDB entry 7kb4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.98Å
Ligands:GOL, PEG, PG4, SO4
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q9KM24_VIBCH

Publication Abstract from PubMed

VxrA and VxrB are cognate histidine kinase (HK) - response regulator (RR) pairs of a two-component signaling system (TCS) found in Vibrio cholerae, a bacterial pathogen that causes cholera. The VxrAB TCS positively regulates virulence, the Type VI Secretion System, biofilm formation, and cell wall homeostasis in V. cholerae, providing protection from environmental stresses and contributing to the transmission and virulence of the pathogen. The VxrA HK has a unique periplasmic sensor domain (SD) and, remarkably, lacks a cytoplasmic linker domain between the second transmembrane helix and the dimerization and histidine phosphotransfer (DHp) domain, indicating that this system may utilize a potentially unique signal sensing and transmission TCS mechanism. In this study, we have determined several crystal structures of VxrA-SD and its mutants. These structures reveal a novel structural fold forming an unusual beta hairpin-swapped dimer. A conformational change caused by relative rotation of the two monomers in a VxrA-SD dimer could potentially change the association of transmembrane helices and, subsequently, the pairing of cytoplasmic DHp domains. Based on the structural observation, we propose a putative scissor-like closing regulation mechanism for the VxrA HK.IMPORTANCE V. cholerae has a dynamic life cycle, which requires rapid adaptation to changing external conditions. Two-component signal transduction (TCS) systems allow V. cholerae to sense and respond to these environmental changes. The VxrAB TCS positively regulates a number of important V. cholerae phenotypes, including virulence, the Type Six Secretion System, biofilm formation, and cell wall homeostasis. Here, we provide the crystal structure of the VxrA sensor histidine kinase sensing domain and propose a mechanism for signal transduction. The cognate signal for VxrAB remains unknown, however, in this work we couple our structural analysis with functional assessments of key residues to further our understanding of this important TCS.

Sensor Domain of Histidine Kinase VxrA of Vibrio cholerae- A Hairpin-swapped Dimer and its Conformational Change.,Tan K, Teschler JK, Wu R, Jedrzejczak RP, Zhou M, Shuvalova LA, Endres MJ, Welk LF, Kwon K, Anderson WF, Satchell KJF, Yildiz FH, Joachimiak A J Bacteriol. 2021 Mar 22. pii: JB.00643-20. doi: 10.1128/JB.00643-20. PMID:33753465[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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References

  1. Tan K, Teschler JK, Wu R, Jedrzejczak RP, Zhou M, Shuvalova LA, Endres MJ, Welk LF, Kwon K, Anderson WF, Satchell KJF, Yildiz FH, Joachimiak A. Sensor Domain of Histidine Kinase VxrA of Vibrio cholerae- A Hairpin-swapped Dimer and its Conformational Change. J Bacteriol. 2021 Mar 22. pii: JB.00643-20. doi: 10.1128/JB.00643-20. PMID:33753465 doi:http://dx.doi.org/10.1128/JB.00643-20

Contents


PDB ID 7la6

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