Crystal structures of the human SUMO-2 protein at 1.6 Å and 1.2 Å resolution: Implication on the functional differences of SUMO proteins

Wen Chen Huang, Tzu Ping Ko, Steven S.L. Li, Andrew H.J. Wang

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55 引文 斯高帕斯(Scopus)

摘要

The SUMO proteins are a class of small ubiquitin-like modifiers. SUMO is attached to a specific lysine side chain on the target protein via an isopeptide bond with its C-terminal glycine. There are at least four SUMO proteins in humans, which are involved in protein trafficking and targeting. A truncated human SUMO-2 protein that contains residues 9-93 was expressed in Escherichia coli and crystallized in two different unit cells, with dimensions of a = b = 75.25 Å, c = 29.17 Å and a = b = 74.96 Å, c = 33.23 Å, both belonging to the rhpmbohedral space group R3. They diffracted X-rays to 1.6 Å and 1.2 Å resolution, respectively. The structures were determined by molecular replacement using the yeast SMT3 protein as a search model. Subsequent refinements yielded R/Rfree values of 0.169/0.190 and 0.119/ 0.185, at 1.6 Å and 1.2 Å, respectively. The peptide folding of SUMO-2 consists of a half-open β-barrel and two flanking α-helices with secondary structural elements arranged as ββαββαβ in the sequence, identical to those of ubiquitin, SMT3 and SUMO-1. Comparison of SUMO-2 with SUMO-1 showed a surface region near the C terminus with significantly different charge distributions. This may explain their distinct intracellular locations. In addition, crystal-packing analysis suggests a possible trimeric assembly of the SUMO-2 protein, of which the biological significance remains to be determined.

原文英語
頁(從 - 到)4114-4122
頁數9
期刊European Journal of Biochemistry
271
發行號20
DOIs
出版狀態已發佈 - 10月 2004
對外發佈

ASJC Scopus subject areas

  • 生物化學

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