 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 4]](mn5082fig4mag.jpg)
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Figure 4
The TgENO1 active site. (a) Superposition of the TgENO1 dimer (green) with the `open-loop' ScENO dimer (blue; PDB entry 1ebh ; Wedekind et al., 1995  ). The r.m.s.d. is 0.56 Å over 777 Cα atoms. (b) Superposition of the TgENO1 dimer with the `closed-loop' hENO1 dimer (orange; PDB entry 3b97
; Kang et al., 2008). The r.m.s.d. is 0.68 Å over 645 Cα atoms. (c) A different perspective of the superposition in (a) highlights the hydrogen bond (dashed line) between the unique TgENO1 residue Glu164 in loop 2 and residue Tyr270 in loop 3. (d) Superposition of TgENO1 on the closed-loop PEP-bound complex (PDB entry 3ucd
; Qin et al., 2012) illustrates that L2 closure necessitates breakage of the Glu164–Tyr270 hydrogen bond and should allow His165 to hydrogen-bond to a PEP O atom. |
![[Figure 4]](mn5082fig4.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
