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PDBsum entry 3lgo

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Protein binding PDB id
3lgo

 

 

 

 

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Contents
Protein chain
140 a.a. *
Waters ×2
* Residue conservation analysis
PDB id:
3lgo
Name: Protein binding
Title: Structure of gse1p, member of the gse/ego complex
Structure: Protein slm4. Chain: a. Synonym: gse complex subunit 1, ego complex subunit 3. Engineered: yes
Source: Saccharomyces cerevisiae. Brewer's yeast,lager beer yeast,yeast. Organism_taxid: 4932. Gene: ego3, gse1, slm4, ybr0723, ybr077c. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
2.85Å     R-factor:   0.317     R-free:   0.351
Authors: K.Kogan,D.Fass
Key ref: K.Kogan et al. (2010). Structural conservation of components in the amino acid sensing branch of the TOR pathway in yeast and mammals. J Mol Biol, 402, 388-398. PubMed id: 20655927
Date:
21-Jan-10     Release date:   04-Aug-10    
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P38247  (SLM4_YEAST) -  Protein SLM4 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc:
162 a.a.
140 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
J Mol Biol 402:388-398 (2010)
PubMed id: 20655927  
 
 
Structural conservation of components in the amino acid sensing branch of the TOR pathway in yeast and mammals.
K.Kogan, E.D.Spear, C.A.Kaiser, D.Fass.
 
  ABSTRACT  
 
The highly conserved Rag family GTPases have a role in reporting amino acid availability to the TOR (target of rapamycin) signaling complex, which regulates cell growth and metabolism in response to environmental cues. The yeast Rag proteins Gtr1p and Gtr2p were shown in multiple independent studies to interact with the membrane-associated proteins Gse1p (Ego3p) and Gse2p (Ego1p). However, mammalian orthologs of Gse1p and Gse2p could not be identified. We determined the crystal structure of Gse1p and found it to match the fold of two mammalian proteins, MP1 (mitogen-activated protein kinase scaffold protein 1) and p14, which form a heterodimeric complex that had been assigned a scaffolding function in mitogen-activated protein kinase pathways. The significance of this structural similarity is validated by the recent identification of a physical and functional association between mammalian Rag proteins and MP1/p14. Together, these findings reveal that key components of the TOR signaling pathway are structurally conserved between yeast and mammals, despite divergence of sequence to a degree that thwarts detection through simple homology searches.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
23361334 J.L.Jewell, R.C.Russell, and K.L.Guan (2013).
Amino acid signalling upstream of mTOR.
  Nat Rev Mol Cell Biol, 14, 133-139.  
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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