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 3
Surface-exposed charged and aromatic residues on KPN03535 that may be functionally important if this protein binds DNA or RNA (for clarity, the view of the monomer shown here is different from that shown in Fig. 4

and was obtained by a 180° rotation around a horizontal axis followed by a 180° rotation around a vertical axis). Arg83, Arg84 and Lys85 comprise the positive surface region described in Fig. 4

. Arg84 and Lys85 are conserved as Arg17 and Lys18 in the E. coli PriB structure and as Arg29 in T. thermophilus aspartyl-tRNA synthetase. Phe94 is conserved in shiga toxin, but there are currently no reports of any functional role of this residue in the toxin.

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

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

doi:10.1107/S1744309109018168

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