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1wm2

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{{STRUCTURE_1wm2| PDB=1wm2 | SCENE= }}
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'''Crystal structure of human SUMO-2 protein'''
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===Crystal structure of human SUMO-2 protein===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_15479240}}
==About this Structure==
==About this Structure==
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[[Category: Two helice]]
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[[Category: Ubiquitin fold]]
[[Category: Ubiquitin fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 04:42:59 2008''

Revision as of 01:43, 28 July 2008

Image:1wm2.png

Template:STRUCTURE 1wm2

Crystal structure of human SUMO-2 protein

Template:ABSTRACT PUBMED 15479240

About this Structure

1WM2 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

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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