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PDBsum entry 3nim
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Metal binding protein
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PDB id
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3nim
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References listed in PDB file
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Key reference
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Title
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Structural basis for the recognition of n-End rule substrates by the ubr box of ubiquitin ligases.
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Authors
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W.S.Choi,
B.C.Jeong,
Y.J.Joo,
M.R.Lee,
J.Kim,
M.J.Eck,
H.K.Song.
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Ref.
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Nat Struct Biol, 2010,
17,
1175-1181.
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PubMed id
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Abstract
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The N-end rule pathway is a regulated proteolytic system that targets proteins
containing destabilizing N-terminal residues (N-degrons) for ubiquitination and
proteasomal degradation in eukaryotes. The N-degrons of type 1 substrates
contain an N-terminal basic residue that is recognized by the UBR box domain of
the E3 ubiquitin ligase UBR1. We describe structures of the UBR box of
Saccharomyces cerevisiae UBR1 alone and in complex with N-degron peptides,
including that of the cohesin subunit Scc1, which is cleaved and targeted for
degradation at the metaphase-anaphase transition. The structures reveal a
previously unknown protein fold that is stabilized by a novel binuclear zinc
center. N-terminal arginine, lysine or histidine side chains of the N-degron are
coordinated in a multispecific binding pocket. Unexpectedly, the structures
together with our in vitro biochemical and in vivo pulse-chase analyses reveal a
previously unknown modulation of binding specificity by the residue at position
2 of the N-degron.
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