1d4x
From Proteopedia
(New page: 200px<br /> <applet load="1d4x" size="450" color="white" frame="true" align="right" spinBox="true" caption="1d4x, resolution 1.75Å" /> '''Crystal Structure o...) |
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| - | [[Image:1d4x.gif|left|200px]]<br /> | + | [[Image:1d4x.gif|left|200px]]<br /><applet load="1d4x" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1d4x" size=" | + | |
caption="1d4x, resolution 1.75Å" /> | caption="1d4x, resolution 1.75Å" /> | ||
'''Crystal Structure of Caenorhabditis Elegans Mg-ATP Actin Complexed with Human Gelsolin Segment 1 at 1.75 A resolution.'''<br /> | '''Crystal Structure of Caenorhabditis Elegans Mg-ATP Actin Complexed with Human Gelsolin Segment 1 at 1.75 A resolution.'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structures of Saccharomyces cerevisiae, Dictyostelium, and | + | The structures of Saccharomyces cerevisiae, Dictyostelium, and Caenorhabditis elegans actin bound to gelsolin segment-1 have been solved and refined at resolutions between 1.9 and 1.75 A. These structures reveal several features relevant to the ATP hydrolytic mechanism, including identification of the nucleophilic water and the roles of Gln-137 and His-161 in positioning and activating the catalytic water, respectively. The involvement of these residues in the catalytic mechanism is consistent with yeast genetics studies. This work highlights both structural and mechanistic similarities with the small and trimeric G proteins and restricts the types of mechanisms responsible for the considerable enhancement of ATP hydrolysis associated with actin polymerization. The conservation of functionalities involved in nucleotide binding and catalysis also provide insights into the mechanistic features of members of the family of actin-related proteins. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1D4X is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MG, CA, SO4, ATP and SO2 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1D4X is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=ATP:'>ATP</scene> and <scene name='pdbligand=SO2:'>SO2</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D4X OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Almo, S | + | [[Category: Almo, S C.]] |
[[Category: Ono, S.]] | [[Category: Ono, S.]] | ||
[[Category: Vorobiev, S.]] | [[Category: Vorobiev, S.]] | ||
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[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: actin]] | [[Category: actin]] | ||
| - | [[Category: c | + | [[Category: c elegans]] |
[[Category: gelsolin s1]] | [[Category: gelsolin s1]] | ||
[[Category: mg-atp]] | [[Category: mg-atp]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:13:07 2008'' |
Revision as of 10:13, 21 February 2008
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Crystal Structure of Caenorhabditis Elegans Mg-ATP Actin Complexed with Human Gelsolin Segment 1 at 1.75 A resolution.
Contents |
Overview
The structures of Saccharomyces cerevisiae, Dictyostelium, and Caenorhabditis elegans actin bound to gelsolin segment-1 have been solved and refined at resolutions between 1.9 and 1.75 A. These structures reveal several features relevant to the ATP hydrolytic mechanism, including identification of the nucleophilic water and the roles of Gln-137 and His-161 in positioning and activating the catalytic water, respectively. The involvement of these residues in the catalytic mechanism is consistent with yeast genetics studies. This work highlights both structural and mechanistic similarities with the small and trimeric G proteins and restricts the types of mechanisms responsible for the considerable enhancement of ATP hydrolysis associated with actin polymerization. The conservation of functionalities involved in nucleotide binding and catalysis also provide insights into the mechanistic features of members of the family of actin-related proteins.
Disease
Known disease associated with this structure: Amyloidosis, Finnish type OMIM:[137350]
About this Structure
1D4X is a Protein complex structure of sequences from Caenorhabditis elegans and Homo sapiens with , , , and as ligands. Full crystallographic information is available from OCA.
Reference
The structure of nonvertebrate actin: implications for the ATP hydrolytic mechanism., Vorobiev S, Strokopytov B, Drubin DG, Frieden C, Ono S, Condeelis J, Rubenstein PA, Almo SC, Proc Natl Acad Sci U S A. 2003 May 13;100(10):5760-5. Epub 2003 May 5. PMID:12732734
Page seeded by OCA on Thu Feb 21 12:13:07 2008
Categories: Caenorhabditis elegans | Homo sapiens | Protein complex | Almo, S C. | Ono, S. | Vorobiev, S. | ATP | CA | MG | SO2 | SO4 | Actin | C elegans | Gelsolin s1 | Mg-atp
