The homodimeric GBS1074 from Streptococcus agalactiae
- 1. School of Biosciences, University of Birmingham, Edgbaston, Birmingham B15 2TT (United Kingdom)
- 2. Birmingham Women's NHS Foundation Trust, Edgbaston, Birmingham B15 2TG (United Kingdom)
Description
The homodimeric nature of the ESAT-6 homologue GBS1074 and the potential for fibre-like assemblies are revealed by the 2 Å resolution crystal structure. 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
Availability note (English)
Available from http://dx.doi.org/10.1107/S1744309110036286; Available from http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3001639Additional details
Identifiers
- URL
- http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3001639;
- DOI
- 10.1107/S1744309110036286;
- PII
- S1744309110036286;
Publishing Information
- Journal Title
- Acta Crystallographica. Section F
- Journal Volume
- 66
- Journal Issue
- Pt 11
- Journal Page Range
- p. 1421-1425
- ISSN
- 1744-3091
- CODEN
- ACSFCL
INIS
- Country of Publication
- United Kingdom
- Country of Input or Organization
- International Atomic Energy Agency (IAEA)
- INIS RN
- 46072713
- Subject category
- S75: CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY;
- Descriptors DEI
- CRYSTAL STRUCTURE; POTENTIALS; PROTEINS; RESOLUTION; STAPHYLOCOCCUS
- Descriptors DEC
- BACTERIA; MICROORGANISMS; ORGANIC COMPOUNDS
Optional Information
- Copyright
- Copyright (c) International Union of Crystallography 2010
- Notes
- PMCID: PMC3001639; PMID: 21045286; PUBLISHER-ID: hv5170; OAI: oai:pubmedcentral.nih.gov:3001639