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PDBsum entry 3kyd
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301 a.a.
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477 a.a.
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77 a.a.
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References listed in PDB file
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Key reference
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Title
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Active site remodelling accompanies thioester bond formation in the sumo e1.
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Authors
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S.K.Olsen,
A.D.Capili,
X.Lu,
D.S.Tan,
C.D.Lima.
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Ref.
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Nature, 2010,
463,
906-912.
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PubMed id
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Abstract
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E1 enzymes activate ubiquitin (Ub) and ubiquitin-like (Ubl) proteins in two
steps by carboxy-terminal adenylation and thioester bond formation to a
conserved catalytic cysteine in the E1 Cys domain. The structural basis for
these intermediates remains unknown. Here we report crystal structures for human
SUMO E1 in complex with SUMO adenylate and tetrahedral intermediate analogues at
2.45 and 2.6 A, respectively. These structures show that side chain contacts to
ATP.Mg are released after adenylation to facilitate a 130 degree rotation of the
Cys domain during thioester bond formation that is accompanied by remodelling of
key structural elements including the helix that contains the E1 catalytic
cysteine, the crossover and re-entry loops, and refolding of two helices that
are required for adenylation. These changes displace side chains required for
adenylation with side chains required for thioester bond formation. Mutational
and biochemical analyses indicate these mechanisms are conserved in other E1s.
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