2gaa: Difference between revisions

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==Overview==

Genome sequencing projects have revealed that P-loop proteins are highly, represented in all organisms and that many of them have no attributed, function. They are characterized by a conserved nucleotide-binding domain, and carry different activities implicated in many cellular processes., Saccharomyces cerevisiae YFH7 is one of these P-loop proteins of unknown, function. In this work we tried to integrate bioinformatics, structure, and enzymology to discover the function of YFH7. Sequence analysis, revealed that yeast YFH7 is a yeast-specific protein showing weak, similarity with the phosphoribulokinase/uridine kinase/bacterial, pantothenate kinase (PRK/URK/PANK) subfamily of P-loop containing kinases., A large insertion of about 100 residues distinguishes YFH7 from other, members of the family. The 1.95 A resolution crystal structure of YFH7, solved using the SAD method confirmed that YFH7 has a fold similar to the, PRK/URK/PANK family, with the characteristic core, lid, and NMP(bind), domains. An additional alpha/beta domain of novel topology corresponds to, the large sequence insertion. Structural and ligand binding analysis, combined with enzymatic assays suggest that YFH7 is an ATP-dependent small, molecule kinase with new substrate specificity. Proteins 2007. (c) 2007, Wiley-Liss, Inc.

Genome sequencing projects have revealed that P-loop proteins are highly represented in all organisms and that many of them have no attributed function. They are characterized by a conserved nucleotide-binding domain and carry different activities implicated in many cellular processes. Saccharomyces cerevisiae YFH7 is one of these P-loop proteins of unknown function. In this work we tried to integrate bioinformatics, structure, and enzymology to discover the function of YFH7. Sequence analysis revealed that yeast YFH7 is a yeast-specific protein showing weak similarity with the phosphoribulokinase/uridine kinase/bacterial pantothenate kinase (PRK/URK/PANK) subfamily of P-loop containing kinases. A large insertion of about 100 residues distinguishes YFH7 from other members of the family. The 1.95 A resolution crystal structure of YFH7 solved using the SAD method confirmed that YFH7 has a fold similar to the PRK/URK/PANK family, with the characteristic core, lid, and NMP(bind) domains. An additional alpha/beta domain of novel topology corresponds to the large sequence insertion. Structural and ligand binding analysis combined with enzymatic assays suggest that YFH7 is an ATP-dependent small molecule kinase with new substrate specificity. Proteins 2007. (c) 2007 Wiley-Liss, Inc.

==About this Structure==

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[[Category: yfr007w]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-Genome sequencing projects have revealed that P-loop proteins are highly, represented in all organisms and that many of them have no attributed, function. They are characterized by a conserved nucleotide-binding domain, and carry different activities implicated in many cellular processes., Saccharomyces cerevisiae YFH7 is one of these P-loop proteins of unknown, function. In this work we tried to integrate bioinformatics, structure, and enzymology to discover the function of YFH7. Sequence analysis, revealed that yeast YFH7 is a yeast-specific protein showing weak, similarity with the phosphoribulokinase/uridine kinase/bacterial, pantothenate kinase (PRK/URK/PANK) subfamily of P-loop containing kinases., A large insertion of about 100 residues distinguishes YFH7 from other, members of the family. The 1.95 A resolution crystal structure of YFH7, solved using the SAD method confirmed that YFH7 has a fold similar to the, PRK/URK/PANK family, with the characteristic core, lid, and NMP(bind), domains. An additional alpha/beta domain of novel topology corresponds to, the large sequence insertion. Structural and ligand binding analysis, combined with enzymatic assays suggest that YFH7 is an ATP-dependent small, molecule kinase with new substrate specificity. Proteins 2007. (c) 2007, Wiley-Liss, Inc.
+Genome sequencing projects have revealed that P-loop proteins are highly represented in all organisms and that many of them have no attributed function. They are characterized by a conserved nucleotide-binding domain and carry different activities implicated in many cellular processes. Saccharomyces cerevisiae YFH7 is one of these P-loop proteins of unknown function. In this work we tried to integrate bioinformatics, structure, and enzymology to discover the function of YFH7. Sequence analysis revealed that yeast YFH7 is a yeast-specific protein showing weak similarity with the phosphoribulokinase/uridine kinase/bacterial pantothenate kinase (PRK/URK/PANK) subfamily of P-loop containing kinases. A large insertion of about 100 residues distinguishes YFH7 from other members of the family. The 1.95 A resolution crystal structure of YFH7 solved using the SAD method confirmed that YFH7 has a fold similar to the PRK/URK/PANK family, with the characteristic core, lid, and NMP(bind) domains. An additional alpha/beta domain of novel topology corresponds to the large sequence insertion. Structural and ligand binding analysis combined with enzymatic assays suggest that YFH7 is an ATP-dependent small molecule kinase with new substrate specificity. Proteins 2007. (c) 2007 Wiley-Liss, Inc.
 ==About this Structure==
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 [[Category: yfr007w]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 11:30:48 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:29:42 2008''