4USX: The Structure Of The C-terminal Yada-like Domain Of Bpsl2063 From Burkholderia Pseudomallei

The 1.8 A resolution crystal structure of a conserved domain of the potential Burkholderia pseudomallei antigen and trimeric autotransporter BPSL2063 is presented as a structural vaccinology target for melioidosis vaccine development. Since BPSL2063 (1090 amino acids) hosts only one conserved domain, and the expression/purification of the full-length protein proved to be problematic, a domain-filtering library was generated using beta-lactamase as a reporter gene to select further BPSL2063 domains. As a result, two domains (D1 and D2) were identified and produced in soluble form in Escherichia coli. Furthermore, as a general tool, a genomic open reading frame-filtering library from the B. pseudomallei genome was also constructed to facilitate the selection of domain boundaries from the entire ORFeome. Such an approach allowed the selection of three potential protein antigens that were also produced in soluble form. The results imply the further development of ORF-filtering methods as a tool in protein-based research to improve the selection and production of soluble proteins or domains for downstream applications such as X-ray crystallography.
PDB ID: 4USXDownload
MMDB ID: 131103
PDB Deposition Date: 2014/7/16
Updated in MMDB: 2015/11
Experimental Method:
x-ray diffraction
Resolution: 1.8  Å
Source Organism:
Similar Structures:
Biological Unit for 4USX: trimeric; determined by author and by software (PISA)
Molecular Components in 4USX
Label Count Molecule
Proteins (3 molecules)
Trimeric Autotransporter Adhesin
Molecule annotation
Chemicals (7 molecules)
* Click molecule labels to explore molecular sequence information.

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