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PDBsum entry 3lgo
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Protein binding
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PDB id
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3lgo
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Contents |
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* Residue conservation analysis
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PDB id:
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Protein binding
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Title:
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Structure of gse1p, member of the gse/ego complex
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Structure:
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Protein slm4. Chain: a. Synonym: gse complex subunit 1, ego complex subunit 3. Engineered: yes
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Source:
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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.
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Resolution:
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2.85Å
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R-factor:
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0.317
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R-free:
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0.351
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Authors:
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K.Kogan,D.Fass
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Key ref:
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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:
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Date:
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21-Jan-10
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Release date:
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04-Aug-10
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PROCHECK
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Headers
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References
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P38247
(SLM4_YEAST) -
Protein SLM4 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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Seq: Struc:
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162 a.a.
140 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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J Mol Biol
402:388-398
(2010)
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PubMed id:
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Structural conservation of components in the amino acid sensing branch of the TOR pathway in yeast and mammals.
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K.Kogan,
E.D.Spear,
C.A.Kaiser,
D.Fass.
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ABSTRACT
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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.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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J.L.Jewell,
R.C.Russell,
and
K.L.Guan
(2013).
Amino acid signalling upstream of mTOR.
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Nat Rev Mol Cell Biol,
14,
133-139.
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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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');
}
}
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