 |
PDBsum entry 3l2k
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Biosynthetic protein
|
PDB id
|
|
|
|
3l2k
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Structure of the d-Alanylgriseoluteic acid biosynthetic protein ehpf, An atypical member of the anl superfamily of adenylating enzymes.
|
|
|
Authors
|
|
A.K.Bera,
V.Atanasova,
S.Gamage,
H.Robinson,
J.F.Parsons.
|
|
|
Ref.
|
|
Acta Crystallogr D Biol Crystallogr, 2010,
66,
664-672.
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
The structure of EhpF, a 41 kDa protein that functions in the biosynthetic
pathway leading to the broad-spectrum antimicrobial compound
D-alanylgriseoluteic acid (AGA), is reported. A cluster of approximately 16
genes, including ehpF, located on a 200 kbp plasmid native to certain strains of
Pantoea agglomerans encodes the proteins that are required for the conversion of
chorismic acid to AGA. Phenazine-1,6-dicarboxylate has been identified as an
intermediate in AGA biosynthesis and deletion of ehpF results in accumulation of
this compound in vivo. The crystallographic data presented here reveal that EhpF
is an atypical member of the acyl-CoA synthase or ANL superfamily of adenylating
enzymes. These enzymes typically catalyze two-step reactions involving
adenylation of a carboxylate substrate followed by transfer of the substrate
from AMP to coenzyme A or another phosphopantetheine. EhpF is distinguished by
the absence of the C-terminal domain that is characteristic of enzymes from this
family and is involved in phosphopantetheine binding and in the second half of
the canonical two-step reaction that is typically observed. Based on the
structure of EhpF and a bioinformatic analysis, it is proposed that EhpF and
EhpG convert phenazine-1,6-dicarboxylate to 6-formylphenazine-1-carboxylate via
an adenylyl intermediate.
|
|
|
|
|
|
|
