Abstract
KPN03535 (gi|152972051) is a putative lipoprotein of unknown function that is secreted by Klebsiella pneumoniae MGH 78578. The crystal structure reveals that despite a lack of any detectable sequence similarity to known structures, it is a novel variant of the OB-fold and structurally similar to the bacterial Cpx-pathway protein NlpE, single-stranded DNA-binding (SSB) proteins and toxins. K. pneumoniae MGH 78578 forms part of the normal human skin, mouth and gut flora and is an opportunistic pathogen that is linked to about 8% of all hospital-acquired infections in the USA. This structure provides the foundation for further investigations into this divergent member of the OB-fold family.
Highlights
KPN03535 is an orphan protein that is exclusively found in Klebsiella pneumoniae MGH 78578 and K. pneumoniae 342
Single-wavelength anomalous diffraction (SAD) data were collected to 2.46 Aresolution on beamline 9-2 at Stanford Synchrotron Radiation Lightsource (SSRL) at the wavelength corresponding to the peak (1) of a selenium absorption edge using the Blu-Ice data-collection environment (McPhillips et al, 2002)
The crystallized protein is comprised of a glycine left after cleavage of the expression and purification tag followed by KPN03535 residues 23–154
Summary
KPN03535 (gi|152972051) is an orphan protein that is exclusively found in Klebsiella pneumoniae MGH 78578 (an opportunistic human pathogen belonging to enterbacteriales of gammaproteobacteria; Galperin et al, 2007; Gill et al, 2006; Frank & Pace, 2008; Ley et al, 2008) and K. pneumoniae 342 (three-residue substitution). It consists of 132 residues with a calculated pI of 9.40 and a predicted signal peptide. Structural comparisons show similarities to the OB-fold-containing Cpx-pathway protein NlpE, single-stranded DNA-binding (SSB) proteins, bacterial OB-fold (BOF) and toxin proteins, which enable inferences about function that may be tested biochemically. This structure should serve as a basis for understanding structure–function relationships in any newly discovered proteins with a similar sequence, such as those identified by whole microbial genome sequencing and metagenomic surveys of the human microbiome
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