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PDBsum entry 2g4d
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Hydrolase/protein binding
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PDB id
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2g4d
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References listed in PDB file
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Key reference
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Title
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Crystal structure of the senp1 mutant c603s-Sumo complex reveals the hydrolytic mechanism of sumo-Specific protease.
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Authors
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Z.Xu,
S.F.Chau,
K.H.Lam,
H.Y.Chan,
T.B.Ng,
S.W.Au.
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Ref.
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Biochem J, 2006,
398,
345-352.
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PubMed id
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Abstract
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SUMO (small ubiquitin-related modifier)-specific proteases catalyse the
maturation and de-conjugation processes of the sumoylation pathway and modulate
various cellular responses including nuclear metabolism and cell cycle
progression. The active-site cysteine residue is conserved among all known
SUMO-specific proteases and is not substitutable by serine in the hydrolysis
reactions demonstrated previously in yeast. We report here that the catalytic
domain of human protease SENP1 (SUMO-specific protease 1) mutant SENP1C(C603S)
carrying a mutation of cysteine to serine at the active site is inactive in
maturation and de-conjugation reactions. To further understand the hydrolytic
mechanism catalysed by SENP1, we have determined, at 2.8 A resolution (1 A = 0.1
nm), the X-ray structure of SENP1C(C603S)-SUMO-1 complex. A comparison of the
structure of SENP2-SUMO-1 suggests strongly that SUMO-specific proteases require
a self-conformational change prior to cleavage of peptide or isopeptide bond in
the maturation and de-conjugation processes respectively. Moreover, analysis of
the interface of SENP1 and SUMO-1 has led to the identification of four unique
amino acids in SENP1 that facilitate the binding of SUMO-1. By means of an in
vitro assay, we further demonstrate a novel function of SENP1 in hydrolysing the
thioester linkage in E1-SUMO and E2-SUMO complexes. The results disclose a new
mechanism of regulation of the sumoylation pathway by the SUMO-specific
proteases.
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Secondary reference #1
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Title
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Mapping residues of sumo precursors essential in differential maturation by sumo-Specific protease, Senp1.
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Authors
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Z.Xu,
S.W.Au.
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Ref.
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Biochem J, 2005,
386,
325-330.
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PubMed id
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