Structure of an essential bacterial protein YeaZ (TM0874) from Thermotoga maritima at 2.5 Å resolution

Xu, Q.; McMullan, D.; Jaroszewski, L.; Krishna, S.S.; Elsliger, M.-A.; Yeh, A.P.; Abdubek, P.; Astakhova, T.; Axelrod, H.L.; Carlton, D.; Chiu, H.-J.; Clayton, T.; Duan, L.; Feuerhelm, J.; Grant, J.C.; Han, G.W.; Jin, K.K.; Klock, H.E.; Knuth, M.W.; Miller, M.D.; Morse, A.T.; Nigoghossian, E.; Okach, L.; Oommachen, S.; Paulsen, J.; Reyes, R.; Rife, C.L.; van den Bedem, H.; Hodgson, K.O.; Wooley, J.; Deacon, A.M.; Godzik, A.; Lesley, S.A.; Wilson, I.A.

doi:10.1107/S1744309109022192

Acta Crystallographica Section F
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

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Figure 4
The conserved residues display large conformational flexibility. (a) Conserved residues on the potential binding surface of TmYeaZ (cyan) and StYeaZ (gray). The C^α positions of these residues are highlighted by spheres. The residues of StYeaZ are labeled in parentheses. (b) A stereoview of the unknown ligand (UNL; shown as red spheres) located between α1 and α2 of TmYeaZ (present in both monomers; the B monomer is shown here). The experimental density for the UNL (after solvent flattening and twofold averaging) is contoured at 1.5σ. Nearby protein residues are shown on stick representation.

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 66| Part 10| October 2010| Pages 1230-1236

doi:10.1107/S1744309109022192

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