7VBS

Structure of the AAA+ ATPase domain of the transcriptional regulator GtrR in Burkholderia cenocepacia

Summary for 7VBS

• Entry DOI: 10.2210/pdb7vbs/pdb
• Descriptor: Sigma-54 dependent trancsriptional regulator, PHOSPHATE ION (3 entities in total)
• Functional Keywords: bacterial enhancer-binding protein, aaa+ atpase, quorum sensing, transcriptional regulator, transcription
• Biological source: Burkholderia cenocepacia
• Total number of polymer chains: 1
• Total formula weight: 51842.65

Authors

Yan, X.F.,Yong, Y.,Gao, Y.G. (deposition date: 2021-09-01, release date: 2021-12-15, Last modification date: 2023-11-29)

Primary citation

Yan, X.F.,Yang, C.,Wang, M.,Yong, Y.,Deng, Y.,Gao, Y.G.
Structural analyses of the AAA+ ATPase domain of the transcriptional regulator GtrR in the BDSF quorum-sensing system in Burkholderia cenocepacia.
Febs Lett., 596:71-80, 2022

PubMed Abstract: Global transcriptional regulator downstream RpfR (GtrR) is a key downstream regulator for quorum-sensing signaling molecule cis-2-dodecenoic acid (BDSF). As a bacterial enhancer-binding protein (bEBP), GtrR is composed of an N-terminal receiver domain, a central ATPases associated with diverse cellular activities (AAA+) ATPase σ -interaction domain, and a C-terminal helix-turn-helix DNA-binding domain. In this work, we solved its AAA+ ATPase domain in both apo and GTP-bound forms. The structure revealed how GtrR specifically recognizes GTP. In addition, we also revealed that GtrR has moderate GTPase activity in vitro in the absence of its activation signal. Finally, we found the residues K170, D236, R311, and R357 in GtrR that are crucial to its biological function, any single mutation leading to completely abolishing GtrR activity.

PubMed: 34837384
DOI: 10.1002/1873-3468.14244

Experimental method

X-RAY DIFFRACTION (1.998 Å)