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PDBsum entry 6ts2
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Protein binding
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PDB id
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6ts2
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PDB id:
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| Name: |
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Protein binding
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Title:
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Truncated version of chaetomium thermophilum udp-glucose glucosyl transferase (uggt) lacking domain trxl2 (417-650).
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Structure:
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Udp-glucose-glycoprotein glucosyltransferase-like protein, udp-glucose-glycoprotein glucosyltransferase-like protein. Chain: a, b, c, d. Engineered: yes. Mutation: yes. Other_details: deletion of ctuggt trxl2 domain i.E. Residues ctuggt 417-650.,Deletion of ctuggt trxl2 domain i.E. Residues ctuggt 417- 650.
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Source:
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Chaetomium thermophilum (strain dsm 1495 / cbs 144.50 / imi 039719). Organism_taxid: 759272. Gene: ctht_0048990. Expressed in: homo sapiens. Expression_system_taxid: 9606. Expression_system_cell: hek293f.
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Resolution:
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5.74Å
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R-factor:
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0.178
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R-free:
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0.249
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Authors:
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P.Roversi,N.Zitzmann
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Key ref:
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C.P.Modenutti
et al.
(2021).
Clamping, bending, and twisting inter-domain motions in the misfold-recognizing portion of UDP-glucose: Glycoprotein glucosyltransferase.
Structure,
29,
357.
PubMed id:
DOI:
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Date:
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19-Dec-19
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Release date:
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08-Jan-20
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PROCHECK
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Headers
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References
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G0SB58
(G0SB58_CHATD) -
UDP-glucose-glycoprotein glucosyltransferase-like protein from Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
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Seq:
Struc:
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1509 a.a.
1111 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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DOI no:
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Structure
29:357
(2021)
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PubMed id:
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Clamping, bending, and twisting inter-domain motions in the misfold-recognizing portion of UDP-glucose: Glycoprotein glucosyltransferase.
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C.P.Modenutti,
J.I.Blanco Capurro,
R.Ibba,
D.S.Alonzi,
M.N.Song,
S.Vasiljević,
A.Kumar,
A.V.Chandran,
G.Tax,
L.Marti,
J.C.Hill,
A.Lia,
M.Hensen,
T.Waksman,
J.Rushton,
S.Rubichi,
A.Santino,
M.A.Martí,
N.Zitzmann,
P.Roversi.
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ABSTRACT
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UDP-glucose:glycoprotein glucosyltransferase (UGGT) flags misfolded
glycoproteins for ER retention. We report crystal structures of full-length
Chaetomium thermophilum UGGT (CtUGGT), two CtUGGT double-cysteine mutants, and
its TRXL2 domain truncation (CtUGGT-ΔTRXL2). CtUGGT molecular dynamics (MD)
simulations capture extended conformations and reveal clamping, bending, and
twisting inter-domain movements. We name "Parodi limit" the maximum
distance on the same glycoprotein between a site of misfolding and an N-linked
glycan that can be reglucosylated by monomeric UGGT in vitro, in response to
recognition of misfold at that site. Based on the MD simulations, we estimate
the Parodi limit as around 70-80 Å. Frequency distributions of distances
between glycoprotein residues and their closest N-linked glycosylation sites in
glycoprotein crystal structures suggests relevance of the Parodi limit to UGGT
activity in vivo. Our data support a "one-size-fits-all adjustable
spanner" UGGT substrate recognition model, with an essential role for the
UGGT TRXL2 domain.
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Links
