3O9O

Crystal Structure of GBS1074, an Esat-6 homologue from Group B Streptococcus

Summary for 3O9O

• Entry DOI: 10.2210/pdb3o9o/pdb
• Descriptor: Uncharacterized protein gbs1074 (2 entities in total)
• Functional Keywords: wxg100, 4-helix bundle, putative virulence factor, putative secreted protein, unknown function
• Biological source: Streptococcus agalactiae
• Total number of polymer chains: 2
• Total formula weight: 24200.47

Authors

White, S.A.,Shukla, A.,Anthony, M. (deposition date: 2010-08-04, release date: 2010-11-10, Last modification date: 2024-02-21)

Primary citation

Shukla, A.,Pallen, M.,Anthony, M.,White, S.A.
The homodimeric GBS1074 from Streptococcus agalactiae.
Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun., 66:1421-1425, 2010

PubMed Abstract: ESAT-6 is a well characterized secreted protein from Mycobacterium tuberculosis and represents the archetype of the WXG100 family of proteins. Genes encoding ESAT-6 homologues have been identified in the genome of the human pathogen Streptococcus agalactiae; one of these genes, esxA, has been cloned and the recombinant protein has been crystallized. In contrast to M. tuberculosis ESAT-6, the crystal structure of GBS1074 reveals a homodimeric structure similar to homologous structures from Staphylococcus aureus and Helicobacter pylori. Intriguingly, GBS1074 forms elongated fibre-like assemblies in the crystal structure.

PubMed: 21045286
DOI: 10.1107/S1744309110036286

Experimental method

X-RAY DIFFRACTION (2 Å)