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PDBsum entry 2g0c

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Hydrolase PDB id
2g0c

 

 

 

 

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Contents
Protein chain
68 a.a. *
Ligands
SO4 ×2
Waters ×48
* Residue conservation analysis
PDB id:
2g0c
Name: Hydrolase
Title: Structure of the RNA binding domain (residues 404-479) of the bacillus subtilis yxin protein
Structure: Atp-dependent RNA helicase dbpa. Chain: a. Fragment: RNA binding domain. Engineered: yes
Source: Bacillus subtilis. Organism_taxid: 1423. Gene: dbpa, dead. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
1.70Å     R-factor:   0.253     R-free:   0.276
Authors: D.B.Mckay
Key ref: S.Wang et al. (2006). The domain of the Bacillus subtilis DEAD-box helicase YxiN that is responsible for specific binding of 23S rRNA has an RNA recognition motif fold. Rna, 12, 959-967. PubMed id: 16611943
Date:
11-Feb-06     Release date:   18-Apr-06    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P42305  (DBPA_BACSU) -  ATP-dependent RNA helicase DbpA from Bacillus subtilis (strain 168)
Seq:
Struc:
479 a.a.
68 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.6.4.13  - Rna helicase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + H2O = ADP + phosphate + H+
ATP
+ H2O
= ADP
+ phosphate
+ H(+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
Rna 12:959-967 (2006)
PubMed id: 16611943  
 
 
The domain of the Bacillus subtilis DEAD-box helicase YxiN that is responsible for specific binding of 23S rRNA has an RNA recognition motif fold.
S.Wang, Y.Hu, M.T.Overgaard, F.V.Karginov, O.C.Uhlenbeck, D.B.McKay.
 
  ABSTRACT  
 
The YxiN protein of Bacillus subtilis is a member of the DbpA subfamily of prokaryotic DEAD-box RNA helicases. Like DbpA, it binds with high affinity and specificity to segments of 23S ribosomal RNA as short as 32 nucleotides (nt) that include hairpin 92. Several experiments have shown that the 76-residue carboxy-terminal domain of YxiN is responsible for the high-affinity RNA binding. The domain has been crystallized and its structure has been solved to 1.7 Angstroms resolution. The structure reveals an RNA recognition motif (RRM) fold that is found in many eukaryotic RNA binding proteins; the RRM fold was not apparent from the amino acid sequence. The domain has two solvent exposed aromatic residues at sites that correspond to the aromatic residues of the ribonucleoprotein (RNP) motifs RNP1 and RNP2 that are essential for RNA binding in many RRMs. However, mutagenesis of these residues (Tyr404 and Tyr447) to alanine has little effect on RNA affinity, suggesting that the YxiN domain binds target RNAs in a manner that differs from the binding mode commonly found in many eukaryotic RRMs.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21428949 D.Klostermeier (2011).
Single-molecule FRET reveals nucleotide-driven conformational changes in molecular machines and their link to RNA unwinding and DNA supercoiling.
  Biochem Soc Trans, 39, 611-616.  
21437710 V.López-Ramírez, L.D.Alcaraz, G.Moreno-Hagelsieb, and G.Olmedo-Álvarez (2011).
Phylogenetic Distribution and Evolutionary History of Bacterial DEAD-Box Proteins.
  J Mol Evol, 72, 413-431.  
19050012 D.Klostermeier, and M.G.Rudolph (2009).
A novel dimerization motif in the C-terminal domain of the Thermus thermophilus DEAD box helicase Hera confers substantial flexibility.
  Nucleic Acids Res, 37, 421-430.
PDB codes: 3eaq 3ear 3eas
19734347 L.M.Sharpe Elles, M.T.Sykes, J.R.Williamson, and O.C.Uhlenbeck (2009).
A dominant negative mutant of the E. coli RNA helicase DbpA blocks assembly of the 50S ribosomal subunit.
  Nucleic Acids Res, 37, 6503-6514.  
19710183 M.G.Rudolph, and D.Klostermeier (2009).
The Thermus thermophilus DEAD box helicase Hera contains a modified RNA recognition motif domain loosely connected to the helicase core.
  RNA, 15, 1993-2001.
PDB codes: 3i31 3i32
  19255475 M.G.Rudolph, J.G.Wittmann, and D.Klostermeier (2009).
Crystallization and preliminary characterization of the Thermus thermophilus RNA helicase Hera C-terminal domain.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 65, 248-252.  
19747077 M.Hilbert, A.R.Karow, and D.Klostermeier (2009).
The mechanism of ATP-dependent RNA unwinding by DEAD box proteins.
  Biol Chem, 390, 1237-1250.  
19079550 K.N.Rao, S.K.Burley, and S.Swaminathan (2008).
UPF201 archaeal specific family members reveal structural similarity to RNA-binding proteins but low likelihood for RNA-binding function.
  PLoS ONE, 3, e3903.
PDB codes: 2nrq 2nwu 2ogk 2pzz
17986459 L.M.Elles, and O.C.Uhlenbeck (2008).
Mutation of the arginine finger in the active site of Escherichia coli DbpA abolishes ATPase and helicase activity and confers a dominant slow growth phenotype.
  Nucleic Acids Res, 36, 41-50.  
18555681 V.B.Chu, and D.Herschlag (2008).
Unwinding RNA's secrets: advances in the biology, physics, and modeling of complex RNAs.
  Curr Opin Struct Biol, 18, 305-314.  
17311413 J.K.Grohman, M.Del Campo, H.Bhaskaran, P.Tijerina, A.M.Lambowitz, and R.Russell (2007).
Probing the mechanisms of DEAD-box proteins as general RNA chaperones: the C-terminal domain of CYT-19 mediates general recognition of RNA.
  Biochemistry, 46, 3013-3022.  
17328755 L.E.Hoelzle, K.Hoelzle, A.Harder, M.Ritzmann, H.Aupperle, H.A.Schoon, K.Heinritzi, and M.M.Wittenbrink (2007).
First identification and functional characterization of an immunogenic protein in unculturable haemotrophic Mycoplasmas (Mycoplasma suis HspA1).
  FEMS Immunol Med Microbiol, 49, 215-223.  
16935881 I.Iost, and M.Dreyfus (2006).
DEAD-box RNA helicases in Escherichia coli.
  Nucleic Acids Res, 34, 4189-4197.  
  17142894 J.M.Caruthers, Y.Hu, and D.B.McKay (2006).
Structure of the second domain of the Bacillus subtilis DEAD-box RNA helicase YxiN.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 62, 1191-1195.
PDB code: 2hjv
16936318 P.Linder (2006).
Dead-box proteins: a family affair--active and passive players in RNP-remodeling.
  Nucleic Acids Res, 34, 4168-4180.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.

 

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