The structure of LpxD from Pseudomonas aeruginosa at 1.3â
Å resolution.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 67(Pt 7): 749-52, 2011 Jul 01.
Article
en En
| MEDLINE
| ID: mdl-21795786
ABSTRACT
LpxD is a bacterial protein that is part of the biosynthesis pathway of lipid A and is responsible for transferring 3-hydroxymyristic acid from the R-3-hydroxymyristoyl-acyl carrier protein to the 2-OH group of UDP-3-O-(3-hydroxymyristoyl) glucosamine. The crystal structure of LpxD from Pseudomonas aeruginosa has been determined at high resolution (1.3â
Å). The crystal belonged to space group H3, with unit-cell parameters a=b=106.19, c=93.38â
Å, and contained one molecule in the asymmetric unit. The structure was solved by molecular replacement using the known structure of LpxD from Escherichia coli (PDB entry 3eh0) as a search model and was refined to Rwork=16.4% (Rfree=18.5%) using 91,655 reflections. The final protein model includes 355 amino-acid residues (including 16 amino acids from a 20 amino-acid N-terminal His tag), one chloride ion and two ethylene glycol molecules.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Pseudomonas aeruginosa
/
Aciltransferasas
Idioma:
En
Revista:
Acta Crystallogr Sect F Struct Biol Cryst Commun
Año:
2011
Tipo del documento:
Article
País de afiliación:
Estados Unidos