2gaa
From Proteopedia
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{{Structure | {{Structure | ||
|PDB= 2gaa |SIZE=350|CAPTION= <scene name='initialview01'>2gaa</scene>, resolution 1.95Å | |PDB= 2gaa |SIZE=350|CAPTION= <scene name='initialview01'>2gaa</scene>, resolution 1.95Å | ||
- | |SITE= | + | |SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Residue+A+2847'>AC1</scene> |
- | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=CME:S,S-(2-HYDROXYETHYL)THIOCYSTEINE'>CME</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
+ | |DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=PRK09270 frcK], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=COG1072 CoaA]</span> | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2gaa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gaa OCA], [http://www.ebi.ac.uk/pdbsum/2gaa PDBsum], [http://www.fli-leibniz.de/cgi-bin/ImgLib.pl?CODE=1kfv JenaLib], [http://www.rcsb.org/pdb/explore.do?structureId=2gaa RCSB]</span> | ||
}} | }} | ||
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[[Category: Chaptal, V.]] | [[Category: Chaptal, V.]] | ||
[[Category: Morera, S.]] | [[Category: Morera, S.]] | ||
- | [[Category: SO4]] | ||
[[Category: unknown function]] | [[Category: unknown function]] | ||
[[Category: yfh7]] | [[Category: yfh7]] | ||
[[Category: yfr007w]] | [[Category: yfr007w]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 26 10:01:26 2008'' |
Revision as of 08:01, 26 March 2008
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, resolution 1.95Å | |||||||
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Sites: | |||||||
Ligands: | , | ||||||
Domains: | frcK, CoaA | ||||||
Resources: | FirstGlance, OCA, PDBsum, JenaLib, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Crystal structure of YFH7 from Saccharomyces cerevisiae: a putative P-loop containing kinase with a circular permutation.
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.
About this Structure
2GAA is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Crystal structure and functional analysis identify the P-loop containing protein YFH7 of Saccharomyces cerevisiae as an ATP-dependent kinase., Gueguen-Chaignon V, Chaptal V, Lariviere L, Costa N, Lopes P, Morera S, Nessler S, Proteins. 2007 Nov 14;. PMID:18004758
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