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PDBsum entry 2asq
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Protein binding
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PDB id
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2asq
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References listed in PDB file
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Key reference
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Title
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Small ubiquitin-Like modifier (sumo) recognition of a sumo binding motif: a reversal of the bound orientation.
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Authors
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J.Song,
Z.Zhang,
W.Hu,
Y.Chen.
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Ref.
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J Biol Chem, 2005,
280,
40122-40129.
[DOI no: ]
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PubMed id
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Abstract
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Sumoylation has recently been identified as an important mechanism that
regulates protein interactions and localization in essential cellular functions,
such as gene transcription, subnuclear structure formation, viral infection, and
cell cycle progression. A SUMO binding amino acid sequence motif (SBM), which
recognizes the SUMO moiety of modified proteins in sumoylation-dependent
cellular functions, has been consistently identified by several recent studies.
To understand the mechanism of SUMO recognition by the SBM, we have solved the
solution structure of SUMO-1 in complex with a peptide containing the SBM
derived from the protein PIASX (KVDVIDLTIESSSDEEEDPPAKR). Surprisingly, the
structure reveals that the bound orientation of the SBM can reverse depending on
the sequence context. The structure also reveals a novel mechanism of
recognizing target sequences by a ubiquitin-like module. Unlike ubiquitin
binding motifs, which all form helices and bind to the main beta-sheet of
ubiquitin, the SBM forms an extended structure that binds between the
alpha-helix and a beta-strand of SUMO-1. This study provides a clear mechanism
of the SBM sequence variations and its recognition of the SUMO moiety in
sumoylated proteins.
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Figure 2.
FIGURE 2. Solution structure of the PIASX-P·SUMO-1
complex. A, stereo view of the superimposed C[  ]traces
of 10 NMR structures of the PIASX-P·SUMO-1 complex.
SUMO-1 is shown in deep pink, and residues 2-8 and other
residues of the PIASX-P peptide are shown in blue and orange,
respectively. B, stereo view of a ribbon diagram of a
representative structure from the ensemble of NMR structures in
the same orientation. The color code is the same as in A.
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Figure 3.
FIGURE 3. The binding interface of the
PIASX-P·SUMO-1 complex. A, stereo view of a ribbon
diagram of SUMO-1 (pink) in complex with the PIASX-P peptide
(light blue). The side chains of the key interface residues
(from which the intermolecular NOEs were observed) from SUMO-1
are shown in deep pink, and the side chains of residues of
PIASX-P involved in the interaction are shown in blue. B, a
similar view as that shown in A except that SUMO-1 is shown as a
surface representation with hydrophobic and aromatic residues
indicated in green. C, a similar view as in B with the surface
of SUMO-1 color-coded according to the electrostatic potentials.
Red to blue corresponds to negative to positive electrostatic
potentials. The side chains of residues 1-8 of the peptide are
shown with acidic side chains indicated in red, and basic side
chains indicated in blue. The side chains of all others residues
are indicated in green.
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The above figures are
reprinted
by permission from the ASBMB:
J Biol Chem
(2005,
280,
40122-40129)
copyright 2005.
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