Literature summary for 3.5.1.108 extracted from

Gennadios, H.A.; Whittington, D.A.; Li, X.; Fierke, C.A.; Christianson, D.W.
Mechanistic inferences from the binding of ligands to LpxC, a metal-dependent deacetylase (2006), Biochemistry, 45, 7940-7948.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
2.7 A resolution X-ray crystal structure of LpxC complexed with the substrate analogue inhibitor, 1,5-anhydro-2-C-(carboxymethyl-N-hydroxamide)-2-deoxy-3-O-myristoyl-D-glucitol, and the 2.0 A resolution structure of LpxC complexed with imidazole. The X-ray crystal structure of LpxC complexed with 1,5-anhydro-2-C-(carboxymethyl-N-hydroxamide)-2-deoxy-3-O-myristoyl-D-glucitol allows for a detailed examination of the coordination geometry of the catalytic zinc ion and other enzyme-inhibitor interactions in the active site. The hydroxamate group of 1,5-anhydro-2-C-(carboxymethyl-N-hydroxamide)-2-deoxy-3-O-myristoyl-D-glucitol forms a bidentate chelate complex with the zinc ion and makes hydrogen bond interactions with conserved active site residues E78, H265, and T191. The inhibitor C-4 hydroxyl group makes direct hydrogen bond interactions with E197 and H58. Finally, the C-3 myristate moiety of the inhibitor binds in the hydrophobic tunnel of the active site	Aquifex aeolicus

Crystallization (Comment)

Organism

2.7 A resolution X-ray crystal structure of LpxC complexed with the substrate analogue inhibitor, 1,5-anhydro-2-C-(carboxymethyl-N-hydroxamide)-2-deoxy-3-O-myristoyl-D-glucitol, and the 2.0 A resolution structure of LpxC complexed with imidazole. The X-ray crystal structure of LpxC complexed with 1,5-anhydro-2-C-(carboxymethyl-N-hydroxamide)-2-deoxy-3-O-myristoyl-D-glucitol allows for a detailed examination of the coordination geometry of the catalytic zinc ion and other enzyme-inhibitor interactions in the active site. The hydroxamate group of 1,5-anhydro-2-C-(carboxymethyl-N-hydroxamide)-2-deoxy-3-O-myristoyl-D-glucitol forms a bidentate chelate complex with the zinc ion and makes hydrogen bond interactions with conserved active site residues E78, H265, and T191. The inhibitor C-4 hydroxyl group makes direct hydrogen bond interactions with E197 and H58. Finally, the C-3 myristate moiety of the inhibitor binds in the hydrophobic tunnel of the active site

Aquifex aeolicus

Inhibitors

Inhibitors	Comment	Organism	Structure
1,5-anhydro-2-deoxy-2-[2-(hydroxyamino)-2-oxoethyl]-3-O-tetradecanoyl-D-glucitol	the X-ray crystal structure of LpxC complexed with TU-514 allows for a detailed examination of the coordination geometry of the catalytic zinc ion and other enzyme-inhibitor interactions in the active site. The hydroxamate group of TU-514 forms a bidentate chelate complex with the zinc ion and makes hydrogen bond interactions with conserved active site residues E78, H265, and T191. The inhibitor C-4 hydroxyl group makes direct hydrogen bond interactions with E197 and H58. Finally, the C-3 myristate moiety of the inhibitor binds in the hydrophobic tunnel of the active site	Aquifex aeolicus

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Zn2+	the native state of this metallohydrolase may contain a pentacoordinate zinc ion	Aquifex aeolicus

Organism

Organism	UniProt	Comment	Textmining
Aquifex aeolicus	O67648	-	-

Synonyms

Synonyms	Comment	Organism
LpxC	-	Aquifex aeolicus