Open AccessThe homodimeric GBS1074 from Streptococcus agalactiae
Author(s) -
Shukla Anshuman,
Pallen Mark,
Anthony Mark,
White Scott A.
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110036286
Subject(s) - streptococcus agalactiae , streptococcus , microbiology and biotechnology , chemistry , biology , bacteria , paleontology
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.