1wm2
From Proteopedia
(New page: 200px<br /><applet load="1wm2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wm2, resolution 1.6Å" /> '''Crystal structure of ...) |
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| - | [[Image:1wm2.jpg|left|200px]]<br /><applet load="1wm2" size=" | + | [[Image:1wm2.jpg|left|200px]]<br /><applet load="1wm2" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1wm2, resolution 1.6Å" /> | caption="1wm2, resolution 1.6Å" /> | ||
'''Crystal structure of human SUMO-2 protein'''<br /> | '''Crystal structure of human SUMO-2 protein'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The SUMO proteins are a class of small ubiquitin-like modifiers. SUMO is | + | 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 Structure== | ==About this Structure== | ||
| - | 1WM2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1WM2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WM2 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Huang, W | + | [[Category: Huang, W C.]] |
| - | [[Category: Ko, T | + | [[Category: Ko, T P.]] |
| - | [[Category: Li, S | + | [[Category: Li, S S.L.]] |
| - | [[Category: Wang, A | + | [[Category: Wang, A H.J.]] |
[[Category: half-open barrel]] | [[Category: half-open barrel]] | ||
[[Category: two helices]] | [[Category: two helices]] | ||
[[Category: ubiquitin fold]] | [[Category: ubiquitin fold]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:45:54 2008'' |
Revision as of 13:45, 21 February 2008
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Crystal structure of human SUMO-2 protein
Overview
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 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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