1nmd
From Proteopedia
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==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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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Almo, S | + | [[Category: Almo, S C.]] |
[[Category: Condeelis, J.]] | [[Category: Condeelis, J.]] | ||
| - | [[Category: Vorobiev, S | + | [[Category: Vorobiev, S M.]] |
[[Category: Welti, S.]] | [[Category: Welti, S.]] | ||
[[Category: ATP]] | [[Category: ATP]] | ||
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[[Category: gelsolin]] | [[Category: gelsolin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:07:36 2008'' |
Revision as of 12:07, 21 February 2008
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Crystal Structure of D. Discoideum Actin-Gelsolin Segment 1 Complex Crystallized In Presence Of Lithium ATP
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
1NMD is a Protein complex structure of sequences from Dictyostelium discoideum 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
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