3M0E

Crystal structure of the ATP-bound state of Walker B mutant of NtrC1 ATPase domain

Summary for 3M0E

• Entry DOI: 10.2210/pdb3m0e/pdb
• Related: 1NY5 1NY6 1ZY2
• Descriptor: Transcriptional regulator (NtrC family), ADENOSINE-5'-TRIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: aaa+ atpase domain, gaftga loop, arginine finger, sigma54 activator, bacterial enhancer binding protein, bacterial transcription, two-component signal transduction, atp-binding, dna-binding, nucleotide-binding, transcription, transcription regulation, molecular motor
• Biological source: Aquifex aeolicus
• Total number of polymer chains: 7
• Total formula weight: 216724.91

Authors

Chen, B.,Sysoeva, T.A.,Chowdhury, S.,Rusu, M.,Birmanns, S.,Guo, L.,Hanson, J.,Yang, H.,Nixon, B.T. (deposition date: 2010-03-02, release date: 2010-11-03, Last modification date: 2023-09-06)

Primary citation

Chen, B.,Sysoeva, T.A.,Chowdhury, S.,Guo, L.,De Carlo, S.,Hanson, J.A.,Yang, H.,Nixon, B.T.
Engagement of Arginine Finger to ATP Triggers Large Conformational Changes in NtrC1 AAA+ ATPase for Remodeling Bacterial RNA Polymerase.
Structure, 18:1420-1430, 2010

PubMed Abstract: The NtrC-like AAA+ ATPases control virulence and other important bacterial activities through delivering mechanical work to σ54-RNA polymerase to activate transcription from σ54-dependent genes. We report the first crystal structure for such an ATPase, NtrC1 of Aquifex aeolicus, in which the catalytic arginine engages the γ-phosphate of ATP. Comparing the new structure with those previously known for apo and ADP-bound states supports a rigid-body displacement model that is consistent with large-scale conformational changes observed by low-resolution methods. First, the arginine finger induces rigid-body roll, extending surface loops above the plane of the ATPase ring to bind σ54. Second, ATP hydrolysis permits Pi release and retraction of the arginine with a reversed roll, remodeling σ54-RNAP. This model provides a fresh perspective on how ATPase subunits interact within the ring-ensemble to promote transcription, directing attention to structural changes on the arginine-finger side of an ATP-bound interface.

PubMed: 21070941
DOI: 10.1016/j.str.2010.08.018

Experimental method

X-RAY DIFFRACTION (2.63 Å)