The homodimeric GBS1074 from Streptococcus agalactiae

Anshuman Shukla; Mark Pallen; M Anthony; Scott White

doi:10.1107/S1744309110036286

The homodimeric GBS1074 from Streptococcus agalactiae

Anshuman Shukla, Mark Pallen, M Anthony, Scott White

Biosciences

Research output: Contribution to journal › Article

13 Citations (Scopus)

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.

Original language	English
Pages (from-to)	1421-1425
Number of pages	5
Journal	Acta Crystallographica Section F Structural Biology and Crystallization Communications
Volume	66
DOIs	https://doi.org/10.1107/S1744309110036286
Publication status	Published - 1 Nov 2010

Keywords

ESAT-6
WXG100
GBS1074
four-helix bundle

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1107/S1744309110036286

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title = "The homodimeric GBS1074 from Streptococcus agalactiae",

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.",

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T1 - The homodimeric GBS1074 from Streptococcus agalactiae

AU - Shukla, Anshuman

AU - Pallen, Mark

AU - Anthony, M

AU - White, Scott

PY - 2010/11/1

Y1 - 2010/11/1

N2 - 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.

AB - 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.

KW - ESAT-6

KW - WXG100

KW - GBS1074

KW - four-helix bundle

U2 - 10.1107/S1744309110036286

DO - 10.1107/S1744309110036286

M3 - Article

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SN - 1744-3091

VL - 66

SP - 1421

EP - 1425

JO - Acta Crystallographica Section F Structural Biology and Crystallization Communications

JF - Acta Crystallographica Section F Structural Biology and Crystallization Communications

ER -

The homodimeric GBS1074 from Streptococcus agalactiae

Abstract

Keywords

UN SDGs

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