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PDBsum entry 4xgt

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Hydrolase PDB id
4xgt

 

 

 

 

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Contents
Protein chain
961 a.a.
Waters ×18
PDB id:
4xgt
Name: Hydrolase
Title: Structure of RNA helicase frh a critical component of the neurospora crassa circadian clock
Structure: Frq-interacting RNA helicase. Chain: a. Fragment: residues 114-1106. Synonym: probable atp dependent RNA helicase. Engineered: yes
Source: Neurospora crassa. Organism_taxid: 5141. Gene: b9b11.040, frh, ncu03363.1. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
3.09Å     R-factor:   0.235     R-free:   0.295
Authors: K.S.Conrad,B.C.Crane
Key ref: K.S.Conrad et al. (2016). Structure of the frequency-interacting RNA helicase: a protein interaction hub for the circadian clock. Embo J, 35, 1707-1719. PubMed id: 27340124 DOI: 10.15252/embj.201694327
Date:
02-Jan-15     Release date:   06-Jul-16    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q873J5  (Q873J5_NEUCS) -  FRQ-interacting RNA helicase from Neurospora crassa
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1106 a.a.
961 a.a.
Key:    PfamA domain  Secondary structure

 

 
DOI no: 10.15252/embj.201694327 Embo J 35:1707-1719 (2016)
PubMed id: 27340124  
 
 
Structure of the frequency-interacting RNA helicase: a protein interaction hub for the circadian clock.
K.S.Conrad, J.M.Hurley, J.Widom, C.S.Ringelberg, J.J.Loros, J.C.Dunlap, B.R.Crane.
 
  ABSTRACT  
 
In the Neurospora crassa circadian clock, a protein complex of frequency (FRQ), casein kinase 1a (CK1a), and the FRQ-interacting RNA Helicase (FRH) rhythmically represses gene expression by the white-collar complex (WCC). FRH crystal structures in several conformations and bound to ADP/RNA reveal differences between FRH and the yeast homolog Mtr4 that clarify the distinct role of FRH in the clock. The FRQ-interacting region at the FRH N-terminus has variable structure in the absence of FRQ A known mutation that disrupts circadian rhythms (R806H) resides in a positively charged surface of the KOW domain, far removed from the helicase core. We show that changes to other similarly located residues modulate interactions with the WCC and FRQ A V142G substitution near the N-terminus also alters FRQ and WCC binding to FRH, but produces an unusual short clock period. These data support the assertion that FRH helicase activity does not play an essential role in the clock, but rather FRH acts to mediate contacts among FRQ, CK1a and the WCC through interactions involving its N-terminus and KOW module.
 

 

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