Crystal structure of YbaK protein from Haemophilus influenzae (HI1434) at 1.8 Å resolution: Functional implications

Hong Zhang, Kui Huang, Zhong Li, Linda Banerjei, Kathryn E. Fisher, Nick V. Grishin, Edward Eisenstein, Osnat Herzberg

Research output: Contribution to journalArticle

44 Citations (Scopus)

Abstract

Structural genomics of proteins of unknown function most straightforwardly assists with assignment of biochemical activity when the new structure resembles that of proteins whose functions are known. When a new fold is revealed, the universe of known folds is enriched, and once the function is determined by other means, novel structure-function relationships are established. The previously unannotated protein HI1434 from H. influenzae provides a hybrid example of these two paradigms. It is a member of a microbial protein family, labeled in SwissProt as YbaK and ebsC. The crystal structure at 1.8 Å resolution reported here reveals a fold that is only remotely related to the C-lectin fold, in particular to endostatin, and thus is not sufficiently similar to imply that YbaK proteins are saccharide binding proteins. However, a crevice that may accommodate a small ligand is evident. The putative binding site contains only one invariant residue, Lys46, which carries a functional group that could play a role in catalysis, indicating that YbaK is probably not an enzyme. Detailed sequence analysis, including a number of newly sequenced microbial organisms, highlights sequence homology to an insertion domain in prolyl-tRNA synthetases (proRS) from prokaryote, a domain whose function is unknown. A HI1434-based model of the insertion domain shows that it should also contain the putative binding site. Being part of a tRNA synthetases, the insertion domain is likely to be involved in oligonucleotide binding, with possible roles in recognition/discrimination or editing of prolyl-tRNA. By analogy, YbaK may also play a role in nucleotide or oligonucleotide binding, the nature of which is yet to be determined. (C) 2000 Wiley-Liss, Inc.

Original languageEnglish (US)
Pages (from-to)86-97
Number of pages12
JournalProteins: Structure, Function and Genetics
Volume40
Issue number1
DOIs
StatePublished - Jul 1 2000

Fingerprint

Crystal structure
Oligonucleotides
Proteins
Binding Sites
Endostatins
Amino Acyl-tRNA Synthetases
Protein Databases
Sequence Homology
Genomics
Transfer RNA
Catalysis
Lectins
Sequence Analysis
Nucleotides
Functional groups
Ligands
Haemophilus influenzae HI1434 protein
Enzymes

Keywords

  • C-lectin fold
  • Circular permutation
  • Hypothetical proteins
  • Structural genomics
  • X-ray crystallography

ASJC Scopus subject areas

  • Genetics
  • Structural Biology
  • Biochemistry

Cite this

Crystal structure of YbaK protein from Haemophilus influenzae (HI1434) at 1.8 Å resolution : Functional implications. / Zhang, Hong; Huang, Kui; Li, Zhong; Banerjei, Linda; Fisher, Kathryn E.; Grishin, Nick V.; Eisenstein, Edward; Herzberg, Osnat.

In: Proteins: Structure, Function and Genetics, Vol. 40, No. 1, 01.07.2000, p. 86-97.

Research output: Contribution to journalArticle

Zhang, Hong ; Huang, Kui ; Li, Zhong ; Banerjei, Linda ; Fisher, Kathryn E. ; Grishin, Nick V. ; Eisenstein, Edward ; Herzberg, Osnat. / Crystal structure of YbaK protein from Haemophilus influenzae (HI1434) at 1.8 Å resolution : Functional implications. In: Proteins: Structure, Function and Genetics. 2000 ; Vol. 40, No. 1. pp. 86-97.
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