1nmd: Difference between revisions

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~~'''~~Crystal Structure of D. Discoideum Actin-Gelsolin Segment 1 Complex Crystallized In Presence Of Lithium ATP~~'''~~

===Crystal Structure of D. Discoideum Actin-Gelsolin Segment 1 Complex Crystallized In Presence Of Lithium ATP===

~~==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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==Disease==

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[[Category: Cytoskeleton organization]]

[[Category: Gelsolin]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 02~~:42:29 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 12:47:36 2008''

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-[[Image:1nmd.jpg|left|200px]]
+{{Seed}}
+[[Image:1nmd.png|left|200px]]
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 {{STRUCTURE_1nmd|  PDB=1nmd  |  SCENE=  }}
-'''Crystal Structure of D. Discoideum Actin-Gelsolin Segment 1 Complex Crystallized In Presence Of Lithium ATP'''
+===Crystal Structure of D. Discoideum Actin-Gelsolin Segment 1 Complex Crystallized In Presence Of Lithium ATP===
-==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 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.
+-->
+{{ABSTRACT_PUBMED_12732734}}
 ==Disease==
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 [[Category: Cytoskeleton organization]]
 [[Category: Gelsolin]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 02:42:29 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 12:47:36 2008''