1yag: Difference between revisions

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==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.

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==

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[[Category: Protein complex]]

[[Category: Saccharomyces cerevisiae]]

[[Category: Almo, S.C.]]

[[Category: Almo, S C.]]

[[Category: Frieden, C.]]

[[Category: Strokopytov, B.]]

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[[Category: gelsolin]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri~~ Feb ~~15 17~~:11:05 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:03:18 2008''

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@@ Line 4: / Line 4: @@
 ==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.
+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==
@@ Line 17: / Line 17: @@
 [[Category: Protein complex]]
 [[Category: Saccharomyces cerevisiae]]
-[[Category: Almo, S.C.]]
+[[Category: Almo, S C.]]
 [[Category: Frieden, C.]]
 [[Category: Strokopytov, B.]]
@@ Line 30: / Line 30: @@
 [[Category: gelsolin]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:11:05 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:03:18 2008''