The structure of SENP1–SUMO-2 complex suggests a structural basis for discrimination between SUMO paralogues during processing
| Autor: | Changjiang Dong, Ronald T. Hay, Linnan Shen, Huanting Liu, James H. Naismith |
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| Rok vydání: | 2006 |
| Předmět: |
Models
Molecular Proteases SENP1 Protein Conformation medicine.medical_treatment Molecular Sequence Data Static Electricity genetic processes SUMO enzymes macromolecular substances Plasma protein binding Biology Crystallography X-Ray environment and public health Biochemistry Substrate Specificity Protein structure Small Ubiquitin-Related Modifier Proteins Endopeptidases medicine Humans Amino Acid Sequence Molecular Biology Peptide sequence Protease Cell Biology Protein Structure Tertiary Cysteine Endopeptidases enzymes and coenzymes (carbohydrates) health occupations Protein Binding Research Article |
| Zdroj: | Biochemical Journal. 397:279-288 |
| ISSN: | 1470-8728 0264-6021 |
| Popis: | The SUMO (small ubiquitin-like modifier)-specific protease SENP1 (sentrin-specific protease 1) can process the three forms of SUMO to their mature forms and deconjugate SUMO from modified substrates. It has been demonstrated previously that SENP1 processed SUMO-1 more efficiently than SUMO-2, but displayed little difference in its ability to deconjugate the different SUMO paralogues from modified substrates. To determine the basis for this substrate specificity, we have determined the crystal structure of SENP1 in isolation and in a transition-state complex with SUMO-2. The interface between SUMO-2 and SENP1 has a relatively poor complementarity, and most of the recognition is determined by interaction between the conserved C-terminus of SUMO-2 and the cleft in the protease. Although SENP1 is rather similar in structure to the related protease SENP2, these proteases have different SUMO-processing activities. Electrostatic analysis of SENP1 in the region where the C-terminal peptide, removed during maturation, would project indicates that it is the electrostatic complementarity between this region of SENP1 and the C-terminal peptides of the various SUMO paralogues that mediates selectivity. |
| Databáze: | OpenAIRE |
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