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![[Figure 2]](gi5016fig2mag.jpg)
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Figure 2
The binding sites for NAD, Mg2+ and malate in AYWB-ME. (a) The binding pocket for NAD (in stick representation) in AYWB-ME. The site for Mg2+ and the proposed malate-binding site are indicated with arrows. Positive to negative electrostatic potential is shown as a red to blue colour ramp mapped onto the solvent-exposed surface. (b) Residues of AYWB-ME involved in electrostatic interactions with NAD. Only residues involved in major contacts are shown. (c) Residues and water molecules at the metal pocket for Mg2+ binding in AYWB-ME. Mg2+ is shown as a small sphere. WAT11–WAT13 correspond to water molecules. (d) Predicted malate-binding site in AYWB-ME based on structural alignment with Human-ME. Residues conserved on binding oxalate (an analogue of the malate substrate) are shown in green stick representation for AYWB-ME and in purple for Human-ME. Below each residue of AYWB-ME, the number of the homologous residue in Human-ME is indicated in parentheses. Tyr36 (yellow stick model) is provided by the other monomer. NAD and oxalate are shown in stick representation and Mg2+ as a small sphere. |
![[Figure 2]](gi5016fig2.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
