1LXA | pdb_00001lxa

UDP N-ACETYLGLUCOSAMINE ACYLTRANSFERASE

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.60 Å
  • R-Value Work: 
    0.184 (Depositor) 

wwPDB Validation   3D Report Full Report


This is version 1.5 of the entry. See complete history. 


Literature

A left-handed parallel beta helix in the structure of UDP-N-acetylglucosamine acyltransferase.

Raetz, C.R., Roderick, S.L.

(1995) Science 270: 997-1000

  • DOI: https://doi.org/10.1126/science.270.5238.997
  • Primary Citation of Related Structures:  
    1LXA

  • PubMed Abstract: 

    UDP-N-acetylglucosamine 3-O-acyltransferase (LpxA) catalyzes the transfer of (R)-3-hydroxymyristic acid from its acyl carrier protein thioester to UDP-N-acetylglucosamine. LpxA is the first enzyme in the lipid A biosynthetic pathway and is a target for the design of antibiotics. The x-ray crystal structure of LpxA has been determined to 2.6 angstrom resolution and reveals a domain motif composed of parallel beta strands, termed a left-handed parallel beta helix (L beta H). This unusual fold displays repeated violations of the protein folding constraint requiring right-handed crossover connections between strands of parallel beta sheets and may be present in other enzymes that share amino acid sequence homology to the repeated hexapeptide motif of LpxA.

    • Organizational Affiliation: 
    • Department of Biochemistry, Duke University Medical Center, Durham, NC 22710, USA.

Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
UDP N-ACETYLGLUCOSAMINE O-ACYLTRANSFERASE262Escherichia coli K-12Mutation(s): 0 
Gene Names: LPXA
EC: 2.3.1.129
UniProt
Find proteins for P0A722 (Escherichia coli (strain K12))
Explore P0A722 
Go to UniProtKB:  P0A722
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP0A722
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.60 Å
  • R-Value Work:  0.184 (Depositor) 
Space Group: P 21 3
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 99α = 90
b = 99β = 90
c = 99γ = 90
Software Package:
Software NamePurpose
X-PLORmodel building
TNTrefinement
X-PLORrefinement
XDSdata reduction
X-PLORphasing

Structure Validation

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View more in-depth experimental data
Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1995-12-07
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Derived calculations, Source and taxonomy, Version format compliance
  • Version 1.3: 2019-07-17
    Changes: Data collection, Other, Refinement description
  • Version 1.4: 2019-08-14
    Changes: Data collection, Refinement description
  • Version 1.5: 2024-02-14
    Changes: Data collection, Database references