4CHX

Crystal structure of MltC in complex with disaccharide pentapeptide DHl89


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.45 Å
  • R-Value Free: 0.248 
  • R-Value Work: 0.192 
  • R-Value Observed: 0.196 

wwPDB Validation 3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

Structure and Cell Wall Cleavage by Modular Lytic Transglycosylase Mltc of Escherichia Coli.

Artola-Recolons, C.Lee, M.Bernardo-Garcia, N.Blazquez, B.Hesek, D.Bartual, S.G.Mahasenan, K.V.Lastochkin, E.Pi, H.Boggess, B.Meindl, K.Uson, I.Fisher, J.F.Mobashery, S.Hermoso, J.A.

(2014) ACS Chem Biol 9: 2058

  • DOI: 10.1021/cb500439c
  • Structures With Same Primary Citation

  • PubMed Abstract: 
  • The lytic transglycosylases are essential bacterial enzymes that catalyze the nonhydrolytic cleavage of the glycan strands of the bacterial cell wall. We describe here the structural and catalytic properties of MltC, one of the seven lytic transglyco ...

    The lytic transglycosylases are essential bacterial enzymes that catalyze the nonhydrolytic cleavage of the glycan strands of the bacterial cell wall. We describe here the structural and catalytic properties of MltC, one of the seven lytic transglycosylases found in the genome of the Gram-negative bacterium Escherichia coli. The 2.3 Å resolution X-ray structure of a soluble construct of MltC shows a unique, compared to known lytic transglycosylase structures, two-domain structure characterized by an expansive active site of 53 Å length extending through an interface between the domains. The structures of three complexes of MltC with cell wall analogues suggest the positioning of the peptidoglycan in the active site both as a substrate and as a product. One complex is suggested to correspond to an intermediate in the course of sequential and exolytic cleavage of the peptidoglycan. Moreover, MltC partitioned its reactive oxocarbenium-like intermediate between trapping by the C6-hydroxyl of the muramyl moiety (lytic transglycosylase activity, the major path) and by water (muramidase activity). Genomic analysis identifies the presence of an MltC homologue in no less than 791 bacterial genomes. While the role of MltC in cell wall assembly and maturation remains uncertain, we propose a functional role for this enzyme as befits the uniqueness of its two-domain structure.


    Organizational Affiliation

    Department of Crystallography and Structural Biology, Inst. Química-Física "Rocasolano", CSIC , Serrano 119, 28006 Madrid, Spain.



Macromolecules

Find similar proteins by: Sequence  |  Structure

Entity ID: 1
MoleculeChainsSequence LengthOrganismDetails
MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE C
A, B
341Escherichia coliMutation(s): 1 
EC: 4.2.2
Find proteins for P0C066 (Escherichia coli (strain K12))
Go to UniProtKB:  P0C066
Protein Feature View
  • Reference Sequence
  • Find similar proteins by: Sequence   |   Structure
Entity ID: 2
MoleculeChainsSequence LengthOrganismDetails
NAG-ANHMUR-PENTAPEPTIDE
C
7synthetic constructMutation(s): 0 
Protein Feature View
  • Reference Sequence
Small Molecules
Modified Residues  1 Unique
IDChainsTypeFormula2D DiagramParent
API
Query on API
CL-PEPTIDE LINKINGC7 H14 N2 O4LYS
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.45 Å
  • R-Value Free: 0.248 
  • R-Value Work: 0.192 
  • R-Value Observed: 0.196 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 50.16α = 90
b = 115β = 93.21
c = 61.28γ = 90
Software Package:
Software NamePurpose
PHENIXmodel building
SCALAdata scaling
iMOSFLMphasing
SCALAphasing
MOLREPphasing
PHENIXphasing
PHENIXrefinement

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History 

  • Version 1.0: 2014-07-23
    Type: Initial release
  • Version 1.1: 2014-10-01
    Changes: Database references