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7VBW

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

Summary for 7VBW
Entry DOI10.2210/pdb7vbw/pdb
DescriptorSigma-54 dependent trancsriptional regulator, GUANOSINE-5'-TRIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
Functional Keywordsbacterial enhancer-binding protein, aaa+ atpase, quorum sensing, transcriptional regulator, transcription
Biological sourceBurkholderia cenocepacia
Total number of polymer chains1
Total formula weight52295.17
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 citationYan, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.5 Å)
Structure validation

239492

數據於2025-07-30公開中

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