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PDBsum entry 3qkf

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Isomerase PDB id
3qkf

 

 

 

 

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Contents
Protein chains
(+ 2 more) 393 a.a.
Ligands
GCO ×8
Metals
_MG ×8
Waters ×3178
Obsolete entry
PDB id:
3qkf
Name: Isomerase
Title: Crystal structure of the mutant p317a of d-mannonate dehydratase from chromohalobacter salexigens complexed with mg and d-gluconate
Structure: Mandelate racemase/muconate lactonizing enzyme. Chain: a, b, c, d, e, f, g, h. Engineered: yes. Mutation: yes
Source: Chromohalobacter salexigens. Organism_taxid: 158080. Gene: csal_2974. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
1.45Å     R-factor:   0.201     R-free:   0.229
Authors: A.A.Fedorov,E.V.Fedorov,D.Wichelecki,J.A.Gerlt,S.C.Almo
Key ref: S.R.Connell et al. (2008). A new tRNA intermediate revealed on the ribosome during EF4-mediated back-translocation. Nat Struct Biol, 15, 910-915. PubMed id: 19172743
Date:
01-Feb-11     Release date:   01-Feb-12    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q1QT89  (DMGD_CHRSD) -  D-galactonate dehydratase family member ManD from Chromohalobacter salexigens (strain ATCC BAA-138 / DSM 3043 / CIP 106854 / NCIMB 13768 / 1H11)
Seq:
Struc:
403 a.a.
393 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 

 
Nat Struct Biol 15:910-915 (2008)
PubMed id: 19172743  
 
 
A new tRNA intermediate revealed on the ribosome during EF4-mediated back-translocation.
S.R.Connell, M.Topf, Y.Qin, D.N.Wilson, T.Mielke, P.Fucini, K.H.Nierhaus, C.M.Spahn.
 
  ABSTRACT  
 
EF4 (LepA) is an almost universally conserved translational GTPase in eubacteria. It seems to be essential under environmental stress conditions and has previously been shown to back-translocate the tRNAs on the ribosome, thereby reverting the canonical translocation reaction. In the current work, EF4 was directly visualized in the process of back-translocating tRNAs by single-particle cryo-EM. Using flexible fitting methods, we built a model of ribosome-bound EF4 based on the cryo-EM map and a recently published unbound EF4 X-ray structure. The cryo-EM map establishes EF4 as a noncanonical elongation factor that interacts not only with the elongating ribosome, but also with the back-translocated tRNA in the A-site region, which is present in a previously unseen, intermediate state and deviates markedly from the position of a canonical A-tRNA. Our results, therefore, provide insight into the underlying structural principles governing back-translocation.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
  22407015 L.Wang, F.Yang, D.Zhang, Z.Chen, R.M.Xu, K.H.Nierhaus, W.Gong, and Y.Qin (2012).
A conserved proline switch on the ribosome facilitates the recruitment and binding of trGTPases.
  Nat Struct Mol Biol, 19, 403-410.  
  19696344 G.Blaha, R.E.Stanley, and T.A.Steitz (2009).
Formation of the first peptide bond: the structure of EF-P bound to the 70S ribosome.
  Science, 325, 966-970.
PDB codes: 3huw 3hux 3huy 3huz
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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