3nbf: Difference between revisions
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==Q28E mutant of hera helicase N-terminal domain bound to 8-oxo-ADP== | ==Q28E mutant of hera helicase N-terminal domain bound to 8-oxo-ADP== | ||
<StructureSection load='3nbf' size='340' side='right' caption='[[3nbf]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='3nbf' size='340' side='right'caption='[[3nbf]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3nbf]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Thet2 Thet2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NBF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3NBF FirstGlance]. <br> | <table><tr><td colspan='2'>[[3nbf]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Thet2 Thet2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NBF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3NBF FirstGlance]. <br> | ||
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</div> | </div> | ||
<div class="pdbe-citations 3nbf" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 3nbf" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[ATPase 3D structures|ATPase 3D structures]] | |||
*[[Helicase 3D structures|Helicase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Thet2]] | [[Category: Thet2]] | ||
[[Category: Klostermeier, D]] | [[Category: Klostermeier, D]] |
Revision as of 21:13, 14 August 2019
Q28E mutant of hera helicase N-terminal domain bound to 8-oxo-ADPQ28E mutant of hera helicase N-terminal domain bound to 8-oxo-ADP
Structural highlights
Publication Abstract from PubMedAbstract DEAD-box proteins disrupt or remodel RNA and protein/RNA complexes at the expense of ATP. The catalytic core is composed of two flexibly connected RecA-like domains. The N-terminal domain contains most of the motifs involved in nucleotide binding and serves as a minimalistic model for helicase/nucleotide interactions. A single conserved glutamine in the so-called Q-motif has been suggested as a conformational sensor for the nucleotide state. To reprogram the Thermus thermophilus RNA helicase Hera for use of oxo-ATP instead of ATP and to investigate the sensor function of the Q-motif, we analyzed helicase activity of Hera Q28E. Crystal structures of the Hera N-terminal domain Q28E mutant (TthDEAD_Q28E) in apo- and ligand-bound forms show that Q28E does change specificity from adenine to 8-oxoadenine. However, significant structural changes accompany the Q28E mutation, which prevent the P-loop from adopting its catalytically active conformation and explain the lack of helicase activity of Hera_Q28E with either ATP or 8-oxo-ATP as energy sources. 8-Oxo-adenosine, 8-oxo-AMP, and 8-oxo-ADP weakly bind to TthDEAD_Q28E but in non-canonical modes. These results indicate that the Q-motif not only senses the nucleotide state of the helicase but could also stabilize a catalytically competent conformation of the P-loop and other helicase signature motifs. Changing nucleotide specificity of the DEAD-box helicase Hera abrogates communication between the Q-motif and the P-loop.,Strohmeier J, Hertel I, Diederichsen U, Rudolph MG, Klostermeier D Biol Chem. 2011 Apr;392(4):357-69. PMID:21391900[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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