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Figure 3.
A, overlay of the active site of E. coli wtGSb (in yellow and
atom colored) and E377A (in green). B, structural comparison of
ADP, glucose binding site, and active site residues between EcGS
(in yellow and atom colored, wtGSb), MalP (blue, PDB 2asv),
rabbit R-GP (pink, PDB 1gpa), OtsA (green, 1uqu), WaaG (orange,
PDB 2iw1), and AGT (cyan, PDB 1y6f). MalP PO[43]^ā, ASO, and
maltopentaose occupied the equivalent positions of the ADP
distal phosphate group, glucose, and HEPPSO in the wtGSb
structure, respectively. Residues are labeled according to EcGS
sequence except for AGT Glu-306. Structural alignment again
using TURBO-FRODO and the CĪ± carbons of the active site
residues. C, left, overlay of NDP-sugar in OtsA, AGT, WaaG, and
ADP and glucose in wtGSb. The color scheme and PDB used are the
same as described in B. Right, comparison of ligands in MalP
(PDB 2asv, blue, PLP + PO[4]^3ā + ASO and PDB 1l5v, red, PLP +
Glc-1-P, in sticks) and in GP (PDB 1noi, lemon, PLP + PO[4]^3ā
+ nojirimycine tetrazole; PDB 2gpb, teal, PLP + glucose; PDB
3gpb, pink, PLP + Glc-1-P, in lines).
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