1yag: Difference between revisions

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[[Image:1yag.jpg|left|200px]]
{{Seed}}
[[Image:1yag.png|left|200px]]


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{{STRUCTURE_1yag|  PDB=1yag  |  SCENE=  }}  
{{STRUCTURE_1yag|  PDB=1yag  |  SCENE=  }}  


'''STRUCTURE OF THE YEAST ACTIN-HUMAN GELSOLIN SEGMENT 1 COMPLEX'''
===STRUCTURE OF THE YEAST ACTIN-HUMAN GELSOLIN SEGMENT 1 COMPLEX===




==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.
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{{ABSTRACT_PUBMED_12732734}}


==About this Structure==
==About this Structure==
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[[Category: Contractile protein]]
[[Category: Contractile protein]]
[[Category: Gelsolin]]
[[Category: Gelsolin]]
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Revision as of 21:20, 27 July 2008

File:1yag.png

Template:STRUCTURE 1yag

STRUCTURE OF THE YEAST ACTIN-HUMAN GELSOLIN SEGMENT 1 COMPLEX

Template:ABSTRACT PUBMED 12732734

About this Structure

1YAG is a Protein complex structure of sequences from Homo sapiens and Saccharomyces cerevisiae. 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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