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PDBsum entry 4e6t
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PDB id:
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Transferase
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Title:
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Structure of lpxa from acinetobacter baumannii at 1.8a resolution (p212121 form)
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Structure:
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Acyl-[acyl-carrier-protein]--udp-n-acetylglucosamine o- acyltransferase. Chain: a, b, c. Synonym: udp-n-acetylglucosamine acyltransferase. Engineered: yes
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Source:
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Acinetobacter baumannii. Organism_taxid: 470. Gene: lpxa, abtw07_2294. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_cell_line: bl21 (de3)
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Resolution:
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1.80Å
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R-factor:
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0.180
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R-free:
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0.211
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Authors:
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J.Badger,B.Chie-Leon,C.Logan,V.Sridhar,B.Sankaran,P.H.Zwart, V.Nienaber
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Key ref:
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J.Badger
et al.
(2012).
Structure determination of LpxA from the lipopolysaccharide-synthesis pathway of Acinetobacter baumannii.
Acta Crystallogr Sect F Struct Biol Cryst Commun,
68,
1477-1481.
PubMed id:
DOI:
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Date:
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15-Mar-12
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Release date:
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12-Dec-12
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PROCHECK
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Headers
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References
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Enzyme class:
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E.C.2.3.1.129
- acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase.
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Reaction:
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a (3R)-hydroxyacyl-[ACP] + UDP-N-acetyl-alpha-D-glucosamine = a UDP-3- O-[(3R)-3-hydroxyacyl]-N-acetyl-alpha-D-glucosamine + holo-[ACP]
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(3R)-3-hydroxyacyl-[acyl-carrier-protein]
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+
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UDP-N-acetyl-alpha-D- glucosamine
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=
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[acyl-carrier-protein]
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+
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UDP-3-O-(3-hydroxyacylyl)-N- acetyl-alpha-D-glucosamine
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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DOI no:
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Acta Crystallogr Sect F Struct Biol Cryst Commun
68:1477-1481
(2012)
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PubMed id:
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Structure determination of LpxA from the lipopolysaccharide-synthesis pathway of Acinetobacter baumannii.
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J.Badger,
B.Chie-Leon,
C.Logan,
V.Sridhar,
B.Sankaran,
P.H.Zwart,
V.Nienaber.
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ABSTRACT
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Acinetobacter baumannii is a Gram-negative pathogenic bacterium which is
resistant to most currently available antibiotics and that poses a significant
health threat to hospital patients. LpxA is a key enzyme in the biosynthetic
pathway of the lipopolysaccharides that are components of the bacterial outer
membrane. It is a potential target for antibacterial agents that might be used
to fight A. baumannii infections. This paper describes the structure
determination of the apo form of LpxA in space groups P2(1)2(1)2(1) and P6(3).
These crystal forms contained three and one protein molecules in the asymmetric
unit and diffracted to 1.8 and 1.4 Å resolution, respectively. A comparison
of the conformations of the independent protein monomers within and between the
two crystal asymmetric units revealed very little structural variation across
this set of structures. In the P6(3) crystal form the enzymatic site is exposed
and is available for the introduction of small molecules of the type used in
fragment-based drug discovery and structure-based lead optimization.
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