1NYN

Solution NMR Structure of Protein YHR087W from Saccharomyces cerevisiae. Northeast Structural Genomics Consortium Target YTYST425.

Summary for 1NYN

• Entry DOI: 10.2210/pdb1nyn/pdb
• NMR Information: BMRB: 5695
• Descriptor: Hypothetical 12.0 kDa protein in NAM8-GAR1 intergenic region (1 entity in total)
• Functional Keywords: hypothetical protein, structural genomics, psi, protein structure initiative, northeast structural genomics consortium, nesg, unknown function
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Cytoplasm: P38804
• Total number of polymer chains: 1
• Total formula weight: 14194.79

Authors

Cort, J.R.,Yee, A.A.,Arrowsmith, C.H.,Kennedy, M.A.,Northeast Structural Genomics Consortium (NESG) (deposition date: 2003-02-13, release date: 2003-04-08, Last modification date: 2024-05-22)

Primary citation

Savchenko, A.,Krogan, N.,Cort, J.R.,Evdokimova, E.,Lew, J.M.,Yee, A.A.,Sanchez-Pulido, L.,Andrade, M.A.,Bochkarev, A.,Watson, J.D.,Kennedy, M.A.,Greenblatt, J.,Hughes, T.,Arrowsmith, C.H.,Rommens, J.M.,Edwards, A.M.
The Shwachman-Bodian-Diamond syndrome protein family is involved in RNA metabolism.
J.Biol.Chem., 280:19213-19220, 2005

PubMed Abstract: A combination of structural, biochemical, and genetic studies in model organisms was used to infer a cellular role for the human protein (SBDS) responsible for Shwachman-Bodian-Diamond syndrome. The crystal structure of the SBDS homologue in Archaeoglobus fulgidus, AF0491, revealed a three domain protein. The N-terminal domain, which harbors the majority of disease-linked mutations, has a novel three-dimensional fold. The central domain has the common winged helix-turn-helix motif, and the C-terminal domain shares structural homology with known RNA-binding domains. Proteomic analysis of the SBDS sequence homologue in Saccharomyces cerevisiae, YLR022C, revealed an association with over 20 proteins involved in ribosome biosynthesis. NMR structural genomics revealed another yeast protein, YHR087W, to be a structural homologue of the AF0491 N-terminal domain. Sequence analysis confirmed them as distant sequence homologues, therefore related by divergent evolution. Synthetic genetic array analysis of YHR087W revealed genetic interactions with proteins involved in RNA and rRNA processing including Mdm20/Nat3, Nsr1, and Npl3. Our observations, taken together with previous reports, support the conclusion that SBDS and its homologues play a role in RNA metabolism.

PubMed: 15701634
DOI: 10.1074/jbc.M414421200

Experimental method

SOLUTION NMR