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© Research
Publication : Protein science : a publication of the Protein Society

Structural and nucleotide-binding properties of YajQ and YnaF, two Escherichia coli proteins of unknown function

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Protein science : a publication of the Protein Society - 01 Nov 2002

Saveanu C, Miron S, Borza T, Craescu CT, Labesse G, Gagyi C, Popescu A, Schaeffer F, Namane A, Laurent-Winter C, Bârzu O, Gilles AM

Link to Pubmed [PMID] – 12381839

Protein Sci. 2002 Nov;11(11):2551-60

Structural genomics is a new approach in functional assignment of proteins identified via whole-genome sequencing programs. Its rationale is that nonhomologous proteins performing similar or related biological functions might have similar tertiary structure. We used dye pseudoaffinity chromatography, two-dimensional gel electrophoresis, and mass spectrometry to identify two novel Escherichia coli nucleotide-binding proteins, YnaF and YajQ. YnaF exhibited significant sequence identity with MJ0577, an ATP-binding protein from a hyperthermophile (Methanococcus jannaschii), and with UspA, a protein from Haemophilus influenzae that belongs to the Universal Stress Protein family. YnaF conserves the ATP-binding site and the dimeric structure observed in the crystal of MJ0577. The protein YajQ, present in many bacterial genomes, is missing in eukaryotes. In the absence of significant similarities of YajQ to any solved structure, we determined its structural and ligand-binding properties by NMR and isothermal titration calorimetry. We demonstrate that YajQ is composed of two domains, each centered on a beta-sheet, that are connected by two helical segments. NMR studies, corroborated with local sequence conservation among YajQ homologs in various bacteria, indicate that one of the beta-sheets is mostly involved in biological activity.

http://www.ncbi.nlm.nih.gov/pubmed/12381839