Crystal structure of glutamyl-tRNA synthetase from Helicobacter pylori

Davis, D.E.; Ayanlade, J.P.; Laseinde, D.T.; Subramanian, S.; Udell, H.; Lorimer, D.J.; Dranow, D.M.; Edwards, T.E.; Myler, P.J.; Asojo, O.A.

doi:10.1107/S2053230X24011099

Acta Crystallographica Section F
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

IUCr IT WDC

home archive editors for authors for readers submit subscribe open access

view article

Figure 2
Primary-sequence alignment of HpGluRS (PDB entry 6b1p), SmGluRS, BtGluRS and PaGluRS (PDB entry 5tgt). Residues involved in glutamate binding are indicated by green asterisks. The secondary-structure elements are as follows: α-helices are shown as large coils, 3₁₀-helices are shown as small coils labeled η, β-strands are shown as arrows labeled β and β-turns are labeled TT. Identical residues are shown on a red background, with conserved residues in red and conserved regions in blue boxes. This figure was generated using ESPript 3.0 (Gouet et al., 1999