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PDBsum entry 4pyp
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Transport protein
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PDB id
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4pyp
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PDB id:
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| Name: |
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Transport protein
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Title:
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Crystal structure of the human glucose transporter glut1
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Structure:
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Solute carrier family 2, facilitated glucose transporter member 1. Chain: a. Synonym: glucose transporter type 1, erythrocyte/brain, glut-1, hepg2 glucose transporter. Engineered: yes. Mutation: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: slc2a1, glut1. Expressed in: trichoplusia ni. Expression_system_taxid: 7111. Expression_system_cell_line: high five.
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Resolution:
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3.17Å
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R-factor:
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0.234
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R-free:
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0.278
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Authors:
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D.Deng,C.Y.Yan,C.Xu,J.P.Wu,P.C.Sun,M.X.Hu,N.Yan
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Key ref:
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D.Deng
et al.
(2014).
Crystal structure of the human glucose transporter GLUT1.
Nature,
510,
121-125.
PubMed id:
DOI:
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Date:
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27-Mar-14
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Release date:
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21-May-14
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PROCHECK
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Headers
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References
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P11166
(GTR1_HUMAN) -
Solute carrier family 2, facilitated glucose transporter member 1 from Homo sapiens
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Seq:
Struc:
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492 a.a.
447 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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*
PDB and UniProt seqs differ
at 2 residue positions (black
crosses)
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DOI no:
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Nature
510:121-125
(2014)
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PubMed id:
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Crystal structure of the human glucose transporter GLUT1.
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D.Deng,
C.Xu,
P.Sun,
J.Wu,
C.Yan,
M.Hu,
N.Yan.
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ABSTRACT
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The glucose transporter GLUT1 catalyses facilitative diffusion of glucose into
erythrocytes and is responsible for glucose supply to the brain and other
organs. Dysfunctional mutations may lead to GLUT1 deficiency syndrome, whereas
overexpression of GLUT1 is a prognostic indicator for cancer. Despite decades of
investigation, the structure of GLUT1 remains unknown. Here we report the
crystal structure of human GLUT1 at 3.2 Å resolution. The full-length
protein, which has a canonical major facilitator superfamily fold, is captured
in an inward-open conformation. This structure allows accurate mapping and
potential mechanistic interpretation of disease-associated mutations in GLUT1.
Structure-based analysis of these mutations provides an insight into the
alternating access mechanism of GLUT1 and other members of the sugar porter
subfamily. Structural comparison of the uniporter GLUT1 with its bacterial
homologue XylE, a proton-coupled xylose symporter, allows examination of the
transport mechanisms of both passive facilitators and active transporters.
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Links
