1wm3
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Crystal structure of human SUMO-2 protein
OverviewOverview
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 A, c=29.17 A and a=b=74.96 A, c=33.23, A, both belonging to the rhombohedral space group R3. They diffracted, X-rays to 1.6 A and 1.2 A 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 A and 1.2 A, respectively. The peptide folding of, SUMO-2 consists of a half-open beta-barrel and two flanking alpha-helices, with secondary structural elements arranged as, betabetaalphabetabetaalphabeta 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.
About this StructureAbout this Structure
1WM3 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structures of the human SUMO-2 protein at 1.6 A and 1.2 A resolution: implication on the functional differences of SUMO proteins., Huang WC, Ko TP, Li SS, Wang AH, Eur J Biochem. 2004 Oct;271(20):4114-22. PMID:15479240
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