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

نویسندگان

  • Debanu Das
  • Piotr Kozbial
  • Gye Won Han
  • Dennis Carlton
  • Lukasz Jaroszewski
  • Polat Abdubek
  • Tamara Astakhova
  • Herbert L. Axelrod
  • Constantina Bakolitsa
  • Connie Chen
  • Hsiu-Ju Chiu
  • Michelle Chiu
  • Thomas Clayton
  • Marc C. Deller
  • Lian Duan
  • Kyle Ellrott
  • Marc-André Elsliger
  • Dustin Ernst
  • Carol L. Farr
  • Julie Feuerhelm
  • Anna Grzechnik
  • Joanna C. Grant
  • Kevin K. Jin
  • Hope A. Johnson
  • Heath E. Klock
  • Mark W. Knuth
  • S. Sri Krishna
  • Abhinav Kumar
  • David Marciano
  • Daniel McMullan
  • Mitchell D. Miller
  • Andrew T. Morse
  • Edward Nigoghossian
  • Amanda Nopakun
  • Linda Okach
  • Silvya Oommachen
  • Jessica Paulsen
  • Christina Puckett
  • Ron Reyes
  • Christopher L. Rife
  • Natasha Sefcovic
  • Henry J. Tien
  • Christine B. Trame
  • Henry van den Bedem
  • Dana Weekes
  • Tiffany Wooten
  • Qingping Xu
  • Keith O. Hodgson
  • John Wooley
  • Ashley M. Deacon
  • Adam Godzik
  • Scott A. Lesley
  • Ian A. Wilson
چکیده

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.

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عنوان ژورنال:

دوره 66  شماره 

صفحات  -

تاریخ انتشار 2010