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

Das, D.; Kozbial, P.; Han, G.W.; Carlton, D.; Jaroszewski, L.; Abdubek, P.; Astakhova, T.; Axelrod, H.L.; Bakolitsa, C.; Chen, C.; Chiu, H.-J.; Chiu, M.; Clayton, T.; Deller, M.C.; Duan, L.; Ellrott, K.; Elsliger, M.-A.; Ernst, D.; Farr, C.L.; Feuerhelm, J.; Grzechnik, A.; Grant, J.C.; Jin, K.K.; Johnson, H.A.; Klock, H.E.; Knuth, M.W.; Krishna, S.S.; Kumar, A.; Marciano, D.; McMullan, D.; Miller, M.D.; Morse, A.T.; Nigoghossian, E.; Nopakun, A.; Okach, L.; Oommachen, S.; Paulsen, J.; Puckett, C.; Reyes, R.; Rife, C.L.; Sefcovic, N.; Tien, H.J.; Trame, C.B.; van den Bedem, H.; Weekes, D.; Wooten, T.; Xu, Q.; Hodgson, K.O.; Wooley, J.; Deacon, A.M.; Godzik, A.; Lesley, S.A.; Wilson, I.A.

doi:10.1107/S1744309109018168

Acta Crystallographica Section F
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

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Figure 1
Crystal structure of KPN03535. (a) Stereo ribbon representation of the KPN03535 monomer color-coded from the N-terminus (yellow) to the C-terminus (green). The nomenclature for helix α and strands β1–β5 follows that used for the OB-fold (Murzin, 1993

). Helices α−2, α−1 and α0 are unique to KPN03535. (b) Diagram showing the secondary-structure elements of KPN03535 superimposed on the primary amino-acid sequence. Helices and β-strands are indicated. The protein was expressed with a purification tag that was removed, leaving a residual Gly residue at the N-terminus followed by the KPN03535 sequence.

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 66| Part 10| October 2010| Pages 1254-1260

doi:10.1107/S1744309109018168

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