1N6Z

Solution NMR Structure of Protein YML108W from Saccharomyces cerevisiae. A novel member of the split bab fold. Northeast Structural Genomics Consortium Target YT601.

Summary for 1N6Z

• Entry DOI: 10.2210/pdb1n6z/pdb
• Descriptor: Hypothetical 12.3 kDa protein in ZDS2-URA5 intergenic region (1 entity in total)
• Functional Keywords: structural proteomics, structural genomics, ocsp, nesg, protein structure initiative, psi, northeast structural genomics consortium, unknown function
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Total number of polymer chains: 1
• Total formula weight: 12355.08

Authors

Pineda-Lucena, A.,Arrowsmith, C.H.,Northeast Structural Genomics Consortium (NESG) (deposition date: 2002-11-12, release date: 2003-05-06, Last modification date: 2024-05-22)

Primary citation

Pineda-Lucena, A.,Liao, J.C.C.,Cort, J.R.,Yee, A.,Kennedy, M.A.,Edwards, A.M.,Arrowsmith, C.H.
A novel member of the split beta-alpha-beta fold: Solution structure of the hypothetical protein YML108W from Saccharomyces cerevisiae. Ontario Centre for Structural Proteomics target (YST0204_1_105); Northeast Structural Genomics Target (YT601).
PROTEIN SCI., 12:1136-1140, 2003

PubMed Abstract: As part of the Northeast Structural Genomics Consortium pilot project focused on small eukaryotic proteins and protein domains, we have determined the NMR structure of the protein encoded by ORF YML108W from Saccharomyces cerevisiae. YML108W belongs to one of the numerous structural proteomics targets whose biological function is unknown. Moreover, this protein does not have sequence similarity to any other protein. The NMR structure of YML108W consists of a four-stranded beta-sheet with strand order 2143 and two alpha-helices, with an overall topology of betabetaalphabetabetaalpha. Strand beta1 runs parallel to beta4, and beta2:beta1 and beta4:beta3 pairs are arranged in an antiparallel fashion. Although this fold belongs to the split betaalphabeta family, it appears to be unique among this family; it is a novel arrangement of secondary structure, thereby expanding the universe of protein folds.

PubMed: 12717036
DOI: 10.1110/ps.0240903

Experimental method

SOLUTION NMR