journal menu
![[Figure 2]](ag5064fig2mag.jpg)
|
|
Figure 2
Structural alignment of PmUreE with other UreE homologues. (a) Alignment of H. pylori UreE (green, PDB entry 3l9z, r.m.s.d. 2.1 Å, 118 Cα atoms aligned), S. pasteurii UreE (blue, PDB entry 1ear, r.m.s.d. 2.1 Å, 120 Cα atoms aligned) and K. aerogenes (yellow, PDB entry 1gmu, r.m.s.d. 1.1 Å, 134 Cα atoms aligned) against PmUreE (orange). The arrow indicates the additional α-helix in PmUreE and the black circle highlights the position of the conserved histidine residue that sits at the dimer interface. (b) Alignment of the dimeric forms of the UreE homologues [coloured as per (a)] with the nickel-binding site at the dimerization interface featured (inset). (c) An intramolecular secondary nickel-binding site is conserved between PmUreE and KaUreE. |
![[Figure 2]](ag5064fig2.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
access
