Published October 27, 2009 | Version v1
Journal article

The structure of KPN03535 (gi|152972051), a novel putative lipoprotein from Klebsiella pneumoniae, reveals an OB-fold

  • 1. Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Menlo Park, California (United States)
  • 2. Joint Center for Structural Genomics, http://www.jcsg.org (United States)
  • 3. Program on Bioinformatics and Systems Biology, Burnham Institute for Medical Research, La Jolla, California (United States)
  • 4. Department of Molecular Biology, The Scripps Research Institute, La Jolla, California (United States)
  • 5. Center for Research in Biological Systems, University of California, San Diego, La Jolla, California (United States)
  • 6. Protein Sciences Department, Genomics Institute of the Novartis Research Foundation, San Diego, California (United States)
  • 7. Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Menlo Park, California (US)
  • 8. Joint Center for Structural Genomics, http://www.jcsg.org (US)
  • 9. Protein Sciences Department, Genomics Institute of the Novartis Research Foundation, San Diego, California (US)
  • 10. Program on Bioinformatics and Systems Biology, Burnham Institute for Medical Research, La Jolla, California (US)
  • 11. Department of Molecular Biology, The Scripps Research Institute, La Jolla, California (US)
  • 12. Photon Science, SLAC National Accelerator Laboratory, Menlo Park, California (US)
  • 13. Center for Research in Biological Systems, University of California, San Diego, La Jolla, California (US)

Description

KPN03535 is a protein unique to K. pneumoniae. The crystal structure reveals that KPN03535 represents a novel variant of the OB-fold and is likely to be a DNA-binding lipoprotein. 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

Availability note (English)

Available from http://dx.doi.org/10.1107/S1744309109018168; Available from http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2954213

Additional details

Publishing Information

Journal Title
Acta Crystallographica. Section F
Journal Volume
66
Journal Issue
Pt 10
Journal Page Range
p. 1254-1260
ISSN
1744-3091
CODEN
ACSFCL

INIS

Country of Publication
United Kingdom
Country of Input or Organization
International Atomic Energy Agency (IAEA)
INIS RN
46072678
Subject category
S60: APPLIED LIFE SCIENCES;
Descriptors DEI
CRYSTAL STRUCTURE; DNA; PROTEINS
Descriptors DEC
NUCLEIC ACIDS; ORGANIC COMPOUNDS

Optional Information

Copyright
Copyright (c) Das et al. 2010
Notes
PMCID: PMC2954213; PMID: 20944219; PUBLISHER-ID: wd5110; OAI: oai:pubmedcentral.nih.gov:2954213; This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.