2iy1
SENP1 (MUTANT) FULL LENGTH SUMO1
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OverviewOverview
Small ubiquitin-like modifier (SUMO)-specific protease SENP1 processes, SUMO-1, SUMO-2 and SUMO-3 to mature forms and deconjugates them from, modified proteins. To establish the proteolytic mechanism, we determined, structures of catalytically inactive SENP1 bound to SUMO-1-modified, RanGAP1 and to unprocessed SUMO-1. In each case, the scissile peptide bond, is kinked at a right angle to the C-terminal tail of SUMO-1 and has the, cis configuration of the amide nitrogens. SENP1 preferentially processes, SUMO-1 over SUMO-2, but binding thermodynamics of full-length SUMO-1 and, SUMO-2 to SENP1 and K(m) values for processing are very similar. However, k(cat) values differ by 50-fold. Thus, discrimination between unprocessed, SUMO-1 and SUMO-2 by SENP1 is based on a catalytic step rather than, substrate binding and is likely to reflect differences in the ability of, SENP1 to correctly orientate the scissile bonds in SUMO-1 and SUMO-2.
DiseaseDisease
Known diseases associated with this structure: Orofacial cleft 10 OMIM:[601912]
About this StructureAbout this Structure
2IY1 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
SUMO protease SENP1 induces isomerization of the scissile peptide bond., Shen L, Tatham MH, Dong C, Zagorska A, Naismith JH, Hay RT, Nat Struct Mol Biol. 2006 Dec;13(12):1069-77. Epub 2006 Nov 12. PMID:17099698
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