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PDBsum entry 3a5y
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protein ligands Protein-protein interface(s) links
Ligase PDB id
3a5y

 

 

 

 

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Contents
Protein chains
297 a.a. *
312 a.a. *
Ligands
KAA ×4
Waters ×1031
* Residue conservation analysis
PDB id:
3a5y
Name: Ligase
Title: Crystal structure of genx from escherichia coli in complex with lysyladenylate analog
Structure: Putative lysyl-tRNA synthetase. Chain: a, b, c, d. Synonym: genx. Engineered: yes
Source: Escherichia coli. Organism_taxid: 562. Strain: mc4100. Gene: ecs5136, genx. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.90Å     R-factor:   0.171     R-free:   0.219
Authors: T.Sumida,T.Yanagisawa,R.Ishii,S.Yokoyama,Riken Structural Genomics/proteomics Initiative (Rsgi)
Key ref: T.Yanagisawa et al. (2010). A paralog of lysyl-tRNA synthetase aminoacylates a conserved lysine residue in translation elongation factor P. Nat Struct Biol, 17, 1136-1143. PubMed id: 20729861
Date:
17-Aug-09     Release date:   25-Aug-10    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P0A8N7  (EPMA_ECOLI) -  Elongation factor P--(R)-beta-lysine ligase from Escherichia coli (strain K12)
Seq:
Struc: 		325 a.a.
297 a.a.
Protein chains
Pfam   ArchSchema ?
P0A8N7  (EPMA_ECOLI) -  Elongation factor P--(R)-beta-lysine ligase from Escherichia coli (strain K12)
Seq:
Struc: 		325 a.a.
312 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: Chains A, B, C, D: E.C.6.3.1.-  - ?????
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
Nat Struct Biol 17:1136-1143 (2010)
PubMed id: 20729861  
 
 
A paralog of lysyl-tRNA synthetase aminoacylates a conserved lysine residue in translation elongation factor P.
T.Yanagisawa, T.Sumida, R.Ishii, C.Takemoto, S.Yokoyama.
 
  ABSTRACT  
 
No abstract given.

 

Literature references that cite this PDB file's key reference

  PubMed id Reference
  21365687 S.Choi, and J.Choe (2011).
Crystal structure of elongation factor P from Pseudomonas aeruginosa at 1.75 Å resolution.
  Proteins, 79, 1688-1693.  
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.

 

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