3MK3

Crystal structure of Lumazine synthase from Salmonella typhimurium LT2


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.57 Å
  • R-Value Free: 0.264 
  • R-Value Work: 0.226 
  • R-Value Observed: 0.226 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Crystal structure analysis of icosahedral lumazine synthase from Salmonella typhimurium, an antibacterial drug target.

Kumar, P.Singh, M.Karthikeyan, S.

(2011) Acta Crystallogr D Biol Crystallogr 67: 131-139

  • DOI: https://doi.org/10.1107/S0907444910053370
  • Primary Citation of Related Structures:  
    3MK3

  • PubMed Abstract: 

    Riboflavin biosynthesis is an essential pathway in bacteria, in contrast to animals, which obtain riboflavin from their diet. Therefore, the enzymes involved in the riboflavin-biosynthesis pathway are potential targets for the development of antibacterial drugs. Lumazine synthase, an enzyme that is involved in the penultimate step of riboflavin biosynthesis, catalyzes the formation of 6,7-dimethyl-8-ribityllumazine from 3,4-dihydroxy-2-butanone 4-phosphate and 5-amino-6-ribitylamino-2,4-(1H,3H)-pyrimidinedione. Lumazine synthase from Salmonella typhimurium (sLS) has been cloned, overexpressed, purified and was crystallized in three forms, each with different crystal packing. The crystal structure of sLS in the monoclinic space group P2(1) has been determined with 60 subunits per asymmetric unit, packed as an icosahedron, at 3.57 Å resolution. Interestingly, sLS contains an N-terminal proline residue (Pro11) which had previously been suggested to disrupt the formation of the icosohedral assembly. In addition, comparison of the structure of sLS with known orthologous lumazine synthase structures allowed identification of the amino-acid residues involved in substrate binding and catalysis. The sLS structure reported here could serve as a starting point for the development of species-specific antibacterial drugs.


  • Organizational Affiliation

    Institute of Microbial Technology, Council of Scientific and Industrial Research (CSIR), Sector 39-A, Chandigarh 160 036, India.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
6,7-dimethyl-8-ribityllumazine synthase156Salmonella enterica subsp. enterica serovar Typhimurium str. LT2Mutation(s): 0 
Gene Names: ribHSTM0417
EC: 2.5.1.78
UniProt
Find proteins for P66038 (Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720))
Explore P66038 
Go to UniProtKB:  P66038
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP66038
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
SO4
Query on SO4

Download Ideal Coordinates CCD File 
AC [auth M]
AD [auth 7]
AE [auth q]
BC [auth M]
BD [auth 8]
AC [auth M],
AD [auth 7],
AE [auth q],
BC [auth M],
BD [auth 8],
BE [auth q],
CC [auth M],
CD [auth 9],
CE [auth s],
DC [auth O],
DD [auth a],
DE [auth s],
EC [auth P],
ED [auth b],
EE [auth u],
FC [auth P],
FD [auth b],
FE [auth v],
GC [auth Q],
GD [auth b],
GE [auth x],
HC [auth R],
HD [auth d],
HE [auth x],
IB [auth A],
IC [auth R],
ID [auth d],
IE [auth y],
JB [auth B],
JC [auth T],
JD [auth e],
KB [auth B],
KC [auth U],
KD [auth f],
LB [auth B],
LC [auth V],
LD [auth g],
MB [auth D],
MC [auth W],
MD [auth h],
NB [auth D],
NC [auth X],
ND [auth h],
OB [auth E],
OC [auth Y],
OD [auth h],
PB [auth F],
PC [auth Z],
PD [auth i],
QB [auth F],
QC [auth Z],
QD [auth k],
RB [auth G],
RC [auth 1],
RD [auth k],
SB [auth H],
SC [auth 1],
SD [auth l],
TB [auth H],
TC [auth 1],
TD [auth m],
UB [auth I],
UC [auth 2],
UD [auth n],
VB [auth J],
VC [auth 2],
VD [auth o],
WB [auth K],
WC [auth 3],
WD [auth o],
XB [auth L],
XC [auth 5],
XD [auth p],
YB [auth L],
YC [auth 6],
YD [auth p],
ZB [auth L],
ZC [auth 7],
ZD [auth p]
SULFATE ION
O4 S
QAOWNCQODCNURD-UHFFFAOYSA-L
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.57 Å
  • R-Value Free: 0.264 
  • R-Value Work: 0.226 
  • R-Value Observed: 0.226 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 154.234α = 90
b = 151.503β = 97.08
c = 235.032γ = 90
Software Package:
Software NamePurpose
MAR345dtbdata collection
MOLREPphasing
CCP4model building
PHENIXrefinement
HKL-2000data reduction
HKL-2000data scaling
CCP4phasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2011-02-02
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2013-01-23
    Changes: Structure summary
  • Version 1.3: 2023-11-01
    Changes: Data collection, Database references, Derived calculations, Refinement description