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PDBsum entry 4z9s
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References listed in PDB file
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Key reference
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Title
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Tetrameric assembly of monoubiquitin accurately mimics the lys11 polyubiquitin chain structure.
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Authors
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O.Levin-Kravets,
N.Shohat,
G.Prag.
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Ref.
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Biochemistry, 2015,
54,
4704-4710.
[DOI no: ]
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PubMed id
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Abstract
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Specific lysine residues on the ubiquitin surface were selected during the
course of evolution to form different polyubiquitin chain structures that signal
diverse cellular processes. A vast number of ubiquitin receptors specifically
recognize and decode the signals conferred by these polyubiquitin chains. The
mechanisms of formation and the structure of Lys11-linked ubiquitin, which
signals for cell-cycle and innate immune control, have been elucidated. Here, we
present a new crystal structure of monomeric ubiquitin that accurately mimics
one of the structures of Lys11-linked ubiquitin. Analysis of the
ubiquitin:ubiquitin interface demonstrates structural fitness and specificity.
The interaction is exclusively hydrophilic, leaving the Ile44 hydrophobic patch,
a major recognition site for ubiquitin receptors, exposed. These noncovalent
ubiquitin:ubiquitin interactions are nearly identical to those reported for
Lys11-linked ubiquitin and seem to play a significant role in stabilizing the
crystal structure without the isopeptide bond. In vitro cross-linking analysis
with wild-type ubiquitin or its mutants partially mimics the interactions in the
crystal. We suggest that these interactions may play a biological role in
transmitting Lys11-linked ubiquitin chain-type cellular signals.
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Secondary reference #1
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Title
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Lys11-Linked ubiquitin chains adopt compact conformations and are preferentially hydrolyzed by the deubiquitinase cezanne.
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Authors
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A.Bremm,
S.M.Freund,
D.Komander.
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Ref.
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Nat Struct Biol, 2010,
17,
939-947.
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PubMed id
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Secondary reference #2
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Title
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Structure of ubiquitin refined at 1.8 a resolution.
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Authors
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S.Vijay-Kumar,
C.E.Bugg,
W.J.Cook.
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Ref.
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J Mol Biol, 1987,
194,
531-544.
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PubMed id
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