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 2.75&Aring;" /> '''SUMO E1 ACTIVATING ...)
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[[Image:1y8r.gif|left|200px]]<br />
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[[Image:1y8r.gif|left|200px]]<br /><applet load="1y8r" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1y8r" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1y8r, resolution 2.75&Aring;" />
caption="1y8r, resolution 2.75&Aring;" />
'''SUMO E1 ACTIVATING ENZYME SAE1-SAE2-SUMO1-MG-ATP COMPLEX'''<br />
'''SUMO E1 ACTIVATING ENZYME SAE1-SAE2-SUMO1-MG-ATP COMPLEX'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1Y8R is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MG, ZN and ATP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Y8R OCA].
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1Y8R is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=ATP:'>ATP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y8R OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Lima, C.D.]]
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[[Category: Lima, C D.]]
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[[Category: Lois, L.M.]]
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[[Category: Lois, L M.]]
[[Category: ATP]]
[[Category: ATP]]
[[Category: MG]]
[[Category: MG]]
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[[Category: sumo; e1; heterodimer; activating enzyme; ubl]]
[[Category: sumo; e1; heterodimer; activating enzyme; ubl]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:16:21 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:02:54 2008''

Revision as of 14:02, 21 February 2008


1y8r, resolution 2.75Å

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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 , and 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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