PDBsum entry: 1n6z

Structural genomics, unknown function

PDB id: 1n6z

Contents

Protein chain

105 a.a. *

* Residue conservation analysis

PDB id:

1n6z

Name:

Structural genomics, unknown function

Title:

Solution nmr structure of protein yml108w from saccharomyces cerevisiae. A novel member of the split bab fold. Northeast structural genomics consortium target yt601.

Structure:

Hypothetical 12.3 kda protein in zds2-ura5 intergenic region. Chain: a. Fragment: yml108w. Engineered: yes

Source:

Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Gene: yml108w or ym8339.11. Expressed in: escherichia coli. Expression_system_taxid: 562

NMR struc:

10 models

Authors:

A.Pineda-Lucena,C.H.Arrowsmith,Northeast Structural Genomics Consortium (Nesg)

Key ref:

A.Pineda-Lucena et al. (2003). A novel member of the split betaalphabeta fold: Solution structure of the hypothetical protein YML108W from Saccharomyces cerevisiae. Protein Sci, 12, 1136-1140. PubMed id: 12717036 DOI: 10.1110/ps.0240903

Date:

12-Nov-02 Release date: 06-May-03

Protein chain

Q03759  (YMK8_YEAST) -  Uncharacterized protein YML108W

Seq: 105 a.a.

Struc: 105 a.a.

 Gene Ontology (GO) functional annotation 

• Cellular component: cytoplasm (2 terms)

DOI no: 10.1110/ps.0240903

Protein Sci 12:1136-1140 (2003)

PubMed id: 12717036

A novel member of the split betaalphabeta fold: Solution structure of the hypothetical protein YML108W from Saccharomyces cerevisiae.

A.Pineda-Lucena, J.C.Liao, J.R.Cort, A.Yee, M.A.Kennedy, A.M.Edwards, C.H.Arrowsmith.

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.

Selected figure(s)

Figure 2.
Figure 2. Ribbon diagram depicting (A) YML108W, (B) formaldehyde ferredoxin oxidoreductase (PDB accession no. 1B25 [PDB] ), (C) B1 domain of protein G (PDB accession no. 2GB1 [PDB] ), (D) chain E of the Cytoplasmic ß Subunit-T1 Assembly Of Voltage-Dependent K Channels (PDB accession no. 1EXB [PDB] ), (E) carboxy-terminal domain of the Escherichia coli arginine repressor (PDB accession no. 1XXA [PDB] ), and (F) amino-terminal domain of the initiation factor 3 (PDB accession no. 1TIF [PDB] ). The common ß-strands and -helices between YML108W and the other proteins are shown in blue and in red, respectively. Insertions are shown in gray.

The above figure is reprinted by permission from the Protein Society: Protein Sci (2003, 12, 1136-1140) copyright 2003.

Figure was selected by an automated process.