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PDBsum entry 2e3u

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protein links
RNA binding protein PDB id
2e3u
Jmol
Contents
Protein chain
166 a.a. *
Waters ×20
* Residue conservation analysis
PDB id:
2e3u
Name: RNA binding protein
Title: Crystal structure analysis of dim2p from pyrococcus horikosh
Structure: Hypothetical protein ph1566. Chain: a. Synonym: ph-dim2p. Engineered: yes
Source: Pyrococcus horikoshii. Organism_taxid: 70601. Strain: ot3. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.30Å     R-factor:   0.229     R-free:   0.263
Authors: M.Tanokura,M.Z.Jia
Key ref:
M.Z.Jia et al. (2007). Crystal structure of Dim2p: a preribosomal RNA processing factor, from Pyrococcus horikoshii OT3 at 2.30 A. Proteins, 69, 428-432. PubMed id: 17654551 DOI: 10.1002/prot.21381
Date:
29-Nov-06     Release date:   23-Oct-07    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
O59282  (O59282_PYRHO) -  Putative uncharacterized protein PH1566
Seq:
Struc:
219 a.a.
166 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biochemical function     RNA binding     1 term  

 

 
DOI no: 10.1002/prot.21381 Proteins 69:428-432 (2007)
PubMed id: 17654551  
 
 
Crystal structure of Dim2p: a preribosomal RNA processing factor, from Pyrococcus horikoshii OT3 at 2.30 A.
M.Z.Jia, J.Ohtsuka, W.C.Lee, K.Nagata, M.Tanokura.
 
  ABSTRACT  
 
No abstract given.

 
  Selected figure(s)  
 
Figure 1.
Figure 1. (A) A ribbon diagram displaying the overall structure of PH-Dim2p. The -helices, -strands, and 3[10]-helices (labeled as ) are colored yellow, cyan, and red, respectively. The graphic figure was drawn with PyMOL.[13] (B). The topology of PH-Dim2p. Blue columns stand for -helices and red arrows stand for -strands. The N- and C-terminal KH domains are named as KH-1 and -2, respectively.
Figure 3.
Figure 3. The hydrogen bonds, a salt bridge, and hydrophobic interactions formed between the two KH domains, KH-1 and KH-2 of PH-Dim2p. (A) The hydrogen bonds and a salt bridge formed between KH-1 and KH-2. KH-1 and -2 are colored cyan and yellow, respectively. (B) The hydrophobic interactions formed between KH-1 and KH-2. KH-1 and -2 are colored cyan and yellow, respectively. The amino acid residues involved in hydrophobic interactions are colored orange.
 
  The above figures are reprinted by permission from John Wiley & Sons, Inc.: Proteins (2007, 69, 428-432) copyright 2007.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
18755838 E.Vanrobays, A.Leplus, Y.N.Osheim, A.L.Beyer, L.Wacheul, and D.L.Lafontaine (2008).
TOR regulates the subcellular distribution of DIM2, a KH domain protein required for cotranscriptional ribosome assembly and pre-40S ribosome export.
  RNA, 14, 2061-2073.  
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.