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| {{STRUCTURE_1d4x| PDB=1d4x | SCENE= }} | | {{STRUCTURE_1d4x| PDB=1d4x | SCENE= }} |
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| '''Crystal Structure of Caenorhabditis Elegans Mg-ATP Actin Complexed with Human Gelsolin Segment 1 at 1.75 A resolution.'''
| | ===Crystal Structure of Caenorhabditis Elegans Mg-ATP Actin Complexed with Human Gelsolin Segment 1 at 1.75 A resolution.=== |
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| ==Overview==
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| 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. | | The line below this paragraph, {{ABSTRACT_PUBMED_12732734}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 12732734 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_12732734}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Gelsolin s1]] | | [[Category: Gelsolin s1]] |
| [[Category: Mg-atp]] | | [[Category: Mg-atp]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:27:28 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 22:25:41 2008'' |