1y8r
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(New page: 200px<br /> <applet load="1y8r" size="450" color="white" frame="true" align="right" spinBox="true" caption="1y8r, resolution 2.75Å" /> '''SUMO E1 ACTIVATING ...)
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Revision as of 18:09, 12 November 2007
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SUMO E1 ACTIVATING ENZYME SAE1-SAE2-SUMO1-MG-ATP COMPLEX
Overview
E1 enzymes facilitate conjugation of ubiquitin and ubiquitin-like proteins, through adenylation, thioester transfer within E1, and thioester transfer, from E1 to E2 conjugating proteins. Structures of human heterodimeric, Sae1/Sae2-Mg.ATP and Sae1/Sae2-SUMO-1-Mg.ATP complexes were determined at, 2.2 and 2.75 A resolution, respectively. Despite the presence of Mg.ATP, the Sae1/Sae2-SUMO-1-Mg.ATP structure reveals a substrate complex insomuch, as the SUMO C-terminus remains unmodified within the adenylation site and, 35 A from the catalytic cysteine, suggesting that additional changes, within the adenylation site may be required to facilitate chemistry prior, to adenylation and thioester transfer. A mechanism for E2 recruitment to, E1 is suggested by biochemical and genetic data, each of which supports a, direct role for the E1 C-terminal ubiquitin-like domain for E2 recruitment, during conjugation.
About this Structure
1Y8R is a Protein complex structure of sequences from Homo sapiens with MG, ZN and ATP as ligands. Full crystallographic information is available from OCA.
Reference
Structures of the SUMO E1 provide mechanistic insights into SUMO activation and E2 recruitment to E1., Lois LM, Lima CD, EMBO J. 2005 Feb 9;24(3):439-51. Epub 2005 Jan 20. PMID:15660128
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