2d07: Difference between revisions
New page: left|200px<br /> <applet load="2d07" size="450" color="white" frame="true" align="right" spinBox="true" caption="2d07, resolution 2.1Å" /> '''Crystal Structure of... |
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'''Crystal Structure of SUMO-3-modified Thymine-DNA Glycosylase'''<br /> | '''Crystal Structure of SUMO-3-modified Thymine-DNA Glycosylase'''<br /> | ||
==Overview== | ==Overview== | ||
Modification of cellular proteins by the small ubiquitin-like modifier | Modification of cellular proteins by the small ubiquitin-like modifier SUMO is important in regulating various cellular events. Many different nuclear proteins are targeted by SUMO, and the functional consequences of this modification are diverse. For most proteins, however, the functional and structural consequences of modification by specific SUMO isomers are unclear. Conjugation of SUMO to thymine-DNA glycosylase (TDG) induces the dissociation of TDG from its product DNA. Structure determination of the TDG central region conjugated to SUMO-1 previously suggested a mechanism in which the SUMOylation-induced conformational change in the C-terminal region of TDG releases TDG from tight binding to its product DNA. Here, we have determined the crystal structure of the central region of TDG conjugated to SUMO-3. The overall structure of SUMO-3-conjugated TDG is similar to the previously reported structure of TDG conjugated to SUMO-1, despite the relatively low level of amino acid sequence similarity between SUMO-3 and SUMO-1. The two structures revealed that the sequence of TDG that resembles the SUMO-binding motif (SBM) can form an intermolecular beta-sheet with either SUMO-1 or SUMO-3. Structural comparison with the canonical SBM shows that this SBM-like sequence of TDG retains all of the characteristic interactions of the SBM, indicating sequence diversity in the SBM. | ||
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
2D07 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | 2D07 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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=2D07 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Hanaoka, F.]] | [[Category: Hanaoka, F.]] | ||
[[Category: Hiroaki, H.]] | [[Category: Hiroaki, H.]] | ||
[[Category: Jee, J | [[Category: Jee, J G.]] | ||
[[Category: Maita, N.]] | [[Category: Maita, N.]] | ||
[[Category: Saitoh, H.]] | [[Category: Saitoh, H.]] | ||
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[[Category: hydrolase]] | [[Category: hydrolase]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:54:08 2008'' | ||
Revision as of 17:54, 21 February 2008
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Crystal Structure of SUMO-3-modified Thymine-DNA Glycosylase
OverviewOverview
Modification of cellular proteins by the small ubiquitin-like modifier SUMO is important in regulating various cellular events. Many different nuclear proteins are targeted by SUMO, and the functional consequences of this modification are diverse. For most proteins, however, the functional and structural consequences of modification by specific SUMO isomers are unclear. Conjugation of SUMO to thymine-DNA glycosylase (TDG) induces the dissociation of TDG from its product DNA. Structure determination of the TDG central region conjugated to SUMO-1 previously suggested a mechanism in which the SUMOylation-induced conformational change in the C-terminal region of TDG releases TDG from tight binding to its product DNA. Here, we have determined the crystal structure of the central region of TDG conjugated to SUMO-3. The overall structure of SUMO-3-conjugated TDG is similar to the previously reported structure of TDG conjugated to SUMO-1, despite the relatively low level of amino acid sequence similarity between SUMO-3 and SUMO-1. The two structures revealed that the sequence of TDG that resembles the SUMO-binding motif (SBM) can form an intermolecular beta-sheet with either SUMO-1 or SUMO-3. Structural comparison with the canonical SBM shows that this SBM-like sequence of TDG retains all of the characteristic interactions of the SBM, indicating sequence diversity in the SBM.
DiseaseDisease
Known disease associated with this structure: Forebrain defects OMIM:[187395]
About this StructureAbout this Structure
2D07 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of SUMO-3-modified thymine-DNA glycosylase., Baba D, Maita N, Jee JG, Uchimura Y, Saitoh H, Sugasawa K, Hanaoka F, Tochio H, Hiroaki H, Shirakawa M, J Mol Biol. 2006 May 26;359(1):137-47. Epub 2006 Mar 31. PMID:16626738
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