2ju0: Difference between revisions

Revision as of 08:03, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2ju0.png

Template:STRUCTURE 2ju0

Structure of Yeast Frequenin bound to PdtIns 4-kinaseStructure of Yeast Frequenin bound to PdtIns 4-kinase

Template:ABSTRACT PUBMED 17720810

About this StructureAbout this Structure

2JU0 is a Protein complex structure of sequences from Saccharomyces cerevisiae. Full experimental information is available from OCA.

ReferenceReference

Structural insights into activation of phosphatidylinositol 4-kinase (Pik1) by yeast frequenin (Frq1)., Strahl T, Huttner IG, Lusin JD, Osawa M, King D, Thorner J, Ames JB, J Biol Chem. 2007 Oct 19;282(42):30949-59. Epub 2007 Aug 24. PMID:17720810

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-'''Structure of Yeast Frequenin bound to PdtIns 4-kinase'''
+===Structure of Yeast Frequenin bound to PdtIns 4-kinase===
-==Overview==
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-Yeast frequenin (Frq1), a small N-myristoylated EF-hand protein, activates phosphatidylinositol 4-kinase Pik1. The NMR structure of Ca2+-bound Frq1 complexed to an N-terminal Pik1 fragment (residues 121-174) was determined. The Frq1 main chain is similar to that in free Frq1 and related proteins in the same branch of the calmodulin superfamily. The myristoyl group and first eight residues of Frq1 are solvent-exposed, and Ca2+ binds the second, third, and fourth EF-hands, which associate to create a groove with two pockets. The Pik1 peptide forms two helices (125-135 and 156-169) connected by a 20-residue loop. Side chains in the Pik1 N-terminal helix (Val-127, Ala-128, Val-131, Leu-132, and Leu-135) interact with solvent-exposed residues in the Frq1 C-terminal pocket (Leu-101, Trp-103, Val-125, Leu-138, Ile-152, and Leu-155); side chains in the Pik1 C-terminal helix (Ala-157, Ala-159, Leu-160, Val-161, Met-165, and Met-167) contact solvent-exposed residues in the Frq1 N-terminal pocket (Trp-30, Phe-34, Phe-48, Ile-51, Tyr-52, Phe-55, Phe-85, and Leu-89). This defined complex confirms that residues in Pik1 pinpointed as necessary for Frq1 binding by site-directed mutagenesis are indeed sufficient for binding. Removal of the Pik1 N-terminal region (residues 8-760) from its catalytic domain (residues 792-1066) abolishes lipid kinase activity, inconsistent with Frq1 binding simply relieving an autoinhibitory constraint. Deletion of the lipid kinase unique motif (residues 35-110) also eliminates Pik1 activity. In the complex, binding of Ca2+-bound Frq1 forces the Pik1 chain into a U-turn. Frq1 may activate Pik1 by facilitating membrane targeting via the exposed N-myristoyl group and by imposing a structural transition that promotes association of the lipid kinase unique motif with the kinase domain.
+The line below this paragraph, {{ABSTRACT_PUBMED_17720810}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17720810 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_17720810}}
 ==About this Structure==
-JU0 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JU0 OCA].
+JU0 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JU0 OCA].
 ==Reference==
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 [[Category: Transferase]]
 [[Category: Yeast]]
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