2GA8
Crystal structure of YFH7 from Saccharomyces cerevisiae: a putative P-loop containing kinase with a circular permutation.
Summary for 2GA8
| Entry DOI | 10.2210/pdb2ga8/pdb |
| Related | 1UJ2 |
| Descriptor | Hypothetical 39.9 kDa protein, MERCURY (II) ION, SULFATE ION, ... (5 entities in total) |
| Functional Keywords | yfr007w, yfh7, unknown function |
| Biological source | Saccharomyces cerevisiae (baker's yeast) |
| Total number of polymer chains | 1 |
| Total formula weight | 42357.44 |
| Authors | Chaptal, V.,Morera, S. (deposition date: 2006-03-08, release date: 2007-03-20, Last modification date: 2011-07-13) |
| Primary citation | Gueguen-Chaignon, V.,Chaptal, V.,Lariviere, L.,Costa, N.,Lopes, P.,Morera, S.,Nessler, S. Crystal structure and functional analysis identify the P-loop containing protein YFH7 of Saccharomyces cerevisiae as an ATP-dependent kinase. Proteins, 71:804-812, 2007 Cited by PubMed Abstract: 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. PubMed: 18004758DOI: 10.1002/prot.21740 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.775 Å) |
Structure validation
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