The structure of the first representative of Pfam family PF09836 reveals a two-domain organization and suggests involvement in transcriptional regulation

Das, D.; Grishin, N.V.; Kumar, A.; Carlton, D.; Bakolitsa, C.; Miller, M.D.; Abdubek, P.; Astakhova, T.; Axelrod, H.L.; Burra, P.; Chen, C.; Chiu, H.-J.; Chiu, M.; Clayton, T.; Deller, M.C.; Duan, L.; Ellrott, K.; Ernst, D.; Farr, C.L.; Feuerhelm, J.; Grzechnik, A.; Grzechnik, S.K.; Grant, J.C.; Han, G.W.; Jaroszewski, L.; Jin, K.K.; Johnson, H.A.; Klock, H.E.; Knuth, M.W.; Kozbial, P.; Krishna, S.S.; Marciano, D.; McMullan, 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.; Elsliger, M.-A.; Deacon, A.M.; Godzik, A.; Lesley, S.A.; Wilson, I.A.

doi:10.1107/S1744309109022672

Acta Crystallographica Section F
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

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Figure 4
Electrostatic surface of potential NGO1945 dimers. (a) The N-terminal dimer. The monomer on the left is drawn as an electrostatic surface (± kT/e), which highlights the basic patch (Arg36, Arg39, Arg48, Arg54, Lys60, Arg64, Lys66, Arg71 and Arg74) that may be involved in DNA/RNA-binding interactions. This basic region is distinct from the portion involved in the protein–protein interactions that form the dimer. These residues are conserved in many proteins belonging to DUF2063 (Pfam website alignment), suggesting functional importance. (b) The C-terminal dimer. The monomer on the left is represented as an electrostatic surface, which highlights the surface-exposed Lys209 in NGO1945 corresponding to Lys40 that is implicated in Z-DNA binding in vaccinia virus E3L protein. The other E3L protein residues implicated in Z-DNA binding, Arg41, Asn44, Lys45, Tyr48 and Trp66, are not conserved in NGO1945.

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 66| Part 10| October 2010| Pages 1174-1181

doi:10.1107/S1744309109022672

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