 |
PDBsum entry 2g0b
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
(+ 0 more)
188 a.a.
|
|
|
|
|
|
|
|
|
|
|
174 a.a.
|
|
|
|
|
|
|
|
|
|
|
170 a.a.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Feem, An n-Acyl amino acid synthase from an uncultured soil microbe: structure, Mechanism, And acyl carrier protein binding.
|
|
|
Authors
|
|
R.M.Van wagoner,
J.Clardy.
|
|
|
Ref.
|
|
Structure, 2006,
14,
1425-1435.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
Attempts to access antibiotics by capturing biosynthetic genes and pathways
directly from environmental DNA, which is overwhelmingly derived from uncultured
bacteria, have revealed a large and previously unknown family of N-acyl amino
acid synthases (NASs). The structure of the NAS FeeM reveals structural
similarity to the GCN5-related N-acyl transferases and acylhomoserine lactone
synthases. The overall structure has a central beta sheet with alpha helices on
both sides. A bound product at a cleft in the beta sheet identifies the active
site and the structural basis for catalysis, and sequence conservation in this
region indicates a bias for recognition over speed. FeeM interacts with an acyl
carrier protein (FeeL), and the structure, mutagenesis, and enzymatic
measurements reveal that a small hydrophobic pocket in alpha helix 5 dominates
binding of FeeM to FeeL. The structural and mechanistic analyses suggest that
the products of FeeM could be bacterial signaling agents.
|
|
|
|
|
|
|
|
Figure 4.
Figure 4. Divergent Stereoview of the Superposition of the
Active Sites of FeeM and AANAT
The backbone atoms and side
chains believed to be important for catalysis in AANAT are shown
in green. The amide portion (i.e., the bond formed during
catalysis) of the product analog bound to AANAT is shown as a
ball-and-stick model in green. The “proton wire” is shown in
red. FeeM is shown in cyan with the amide portion of N-lauroyl
tyrosine shown as a ball and stick in dark gray.
|
|
Figure 5.
Figure 5. Proposed Mechanism for FeeM
This mechanism
is based on aspects of GNAT function and the similarity between
FeeM and AANAT. The sequence of proton transfers shown, which is
somewhat arbitrary, indicate plausible general bases in the
active site. FeeL is the ACP with which FeeM interacts.
|
|
|
|
|
|
The above figures are
reprinted
by permission from Cell Press:
Structure
(2006,
14,
1425-1435)
copyright 2006.
|
|
|
|
|
|
|
