 |
PDBsum entry 3ryk
|
|
|
|
PDB id:
|
|
|
|
| Name: |
|
Isomerase
|
|
|
Title:
|
|
1.63 angstrom resolution crystal structure of dtdp-4-dehydrorhamnose 3,5-epimerase (rfbc) from bacillus anthracis str. Ames with tdp and ppi bound
|
|
Structure:
|
|
Dtdp-4-dehydrorhamnose 3,5-epimerase. Chain: a, b. Engineered: yes
|
|
Source:
|
|
Bacillus anthracis str. Ames. Anthrax,anthrax bacterium. Organism_taxid: 198094. Strain: bacillus anthracis str. Ames. Gene: bas1136, ba_1229, gbaa_1229, rfbc. Expressed in: escherichia coli. Expression_system_taxid: 469008.
|
|
Resolution:
|
|
|
1.63Å
|
R-factor:
|
0.125
|
R-free:
|
0.160
|
|
|
Authors:
|
|
A.S.Halavaty,M.Kuhn,G.Minasov,L.Shuvalova,K.Kwon,W.F.Anderson,Center For Structural Genomics Of Infectious Diseases (Csgid)
|
|
Key ref:
|
|
A.Shornikov
et al.
(2017).
Structure of the Bacillus anthracis dTDP-L-rhamnose-biosynthetic enzyme dTDP-4-dehydrorhamnose 3,5-epimerase (RfbC).
Acta Crystallogr F Struct Biol Commun,
73,
664-671.
PubMed id:
|
|
|
Date:
|
|
|
11-May-11
|
Release date:
|
25-May-11
|
|
|
|
|
|
|
PROCHECK
|
|
|
|
|
|
Headers
|
|
|
|
References
|
|
|
|
|
|
|
|
A0A6L7H6N0
(A0A6L7H6N0_BACAN) -
dTDP-4-dehydrorhamnose 3,5-epimerase from Bacillus anthracis
|
|
|
|
Seq:
Struc:
|
|
|
|
181 a.a.
175 a.a.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Key: |
 |
PfamA domain |
|
|
 |
Secondary structure |
|
 |
CATH domain |
|
|
|
|
|
|
|
|
|
|
|
|
|
Enzyme class:
|
|
E.C.5.1.3.13
- dTDP-4-dehydrorhamnose 3,5-epimerase.
|
|
|
|
|
|
|
Pathway:
|
|
6-Deoxyhexose Biosynthesis
|
|
|
|
|
|
Reaction:
|
|
dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-4-dehydro-beta-L-rhamnose
|
|
|
|
|
|
dTDP-4-dehydro-6-deoxy-alpha-D-glucose
Bound ligand (Het Group name = )
matches with 71.43% similarity
|
=
|
dTDP-4-dehydro-beta-L-rhamnose
|
|
|
|
|
|
|
|
|
|
Cofactor:
|
|
NAD(+)
|
|
|
|
|
|
NAD(+)
|
|
|
|
|
|
|
Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
| |
|
|
| |
|
|
Acta Crystallogr F Struct Biol Commun
73:664-671
(2017)
|
|
PubMed id:
|
|
|
|
|
|
| |
|
Structure of the Bacillus anthracis dTDP-L-rhamnose-biosynthetic enzyme dTDP-4-dehydrorhamnose 3,5-epimerase (RfbC).
|
|
A.Shornikov,
H.Tran,
J.Macias,
A.S.Halavaty,
G.Minasov,
W.F.Anderson,
M.L.Kuhn.
|
|
|
|
|
| |
ABSTRACT
|
|
|
|
| |
|
|
The exosporium layer of Bacillus anthracis spores is rich in L-rhamnose, a
common bacterial cell-wall component, which often contributes to the virulence
of pathogens by increasing their adherence and immune evasion. The biosynthetic
pathway used to form the activated L-rhamnose donor dTDP-L-rhamnose consists of
four enzymes (RfbA, RfbB, RfbC and RfbD) and is an attractive drug target
because there are no homologs in mammals. It was found that co-purifying and
screening RfbC (dTDP-6-deoxy-D-xylo-4-hexulose 3,5-epimerase) from B. anthracis
in the presence of the other three B. anthracis enzymes of the biosynthetic
pathway yielded crystals that were suitable for data collection. RfbC
crystallized as a dimer and its structure was determined at 1.63 Å
resolution. Two different ligands were bound in the protein structure:
pyrophosphate in the active site of one monomer and dTDP in the other monomer. A
structural comparison with RfbC homologs showed that the key active-site
residues are conserved across kingdoms.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
 |
 |
|
Links
