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 4
Comparison of the electrostatic surface potentials of monomers of (a) NlpE, (b) shiga toxin, (c) BOF, (d) E. coli SSB, (e) E. coli PriB, (f) T. thermophilus aspartyl-tRNA synthetase and (g) KPN03535. All the figures are in approximately the same orientation and reflect the surface view that would be presented for oligonucleotide binding, as in tRNA synthetase. The figure reveals that the positively charged surface patch (central blue portion in black circles) on the KPN03535 most closely resembles that of E. coli PriB and is also similar to that seen in aspartyl-tRNA synthetase. In KPN03535, this positively charged patch is formed by Arg83, Arg84 and Lys85. The corresponding conserved residues are Arg17 and Lys18 in PriB and Arg29 in aspartyl-tRNA synthetases, respectively.

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

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

doi:10.1107/S1744309109018168

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