PDBsum entry 2g0b

Transferase

PDB id: 2g0b

Contents

Protein chains

(+ 0 more) 188 a.a. *

174 a.a. *

170 a.a. *

Ligands

NLT ×8

Waters ×9

* Residue conservation analysis

PDB id:

2g0b

Name:

Transferase

Title:

The structure of feem, an n-acyl amino acid synthase from uncultured soil microbes

Structure:

Feem. Chain: a, b, c, d, e, f, g, h. Engineered: yes

Source:

Uncultured bacterium. Organism_taxid: 77133. Gene: feem. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Biol. unit:

Dimer (from PQS)

Resolution:

3.00Å R-factor: 0.255 R-free: 0.292

Authors:

R.M.Van Wagoner,J.Clardy

Key ref:

R.M.Van Wagoner and J.Clardy (2006). FeeM, an N-acyl amino acid synthase from an uncultured soil microbe: structure, mechanism, and acyl carrier protein binding. Structure, 14, 1425-1435. PubMed id: 16962973 DOI: 10.1016/j.str.2006.07.005

Date:

11-Feb-06 Release date: 26-Sep-06

Protein chains

Q8KNZ7  (Q8KNZ7_9BACT) -  Long-chain N-acyl amino acid synthase from uncultured bacterium CSLC2

Seq: 196 a.a.

Struc: 188 a.a.

Protein chain

Q8KNZ7  (Q8KNZ7_9BACT) -  Long-chain N-acyl amino acid synthase from uncultured bacterium CSLC2

Seq: 196 a.a.

Struc: 174 a.a.

Protein chain

Q8KNZ7  (Q8KNZ7_9BACT) -  Long-chain N-acyl amino acid synthase from uncultured bacterium CSLC2

Seq: 196 a.a.

Struc: 170 a.a.

Enzyme reactions

• Enzyme class: Chains A, B, C, D, E, F, G, H: E.C.2.3.1.- - ?????

DOI no: 10.1016/j.str.2006.07.005

Structure 14:1425-1435 (2006)

PubMed id: 16962973

FeeM, an N-acyl amino acid synthase from an uncultured soil microbe: structure, mechanism, and acyl carrier protein binding.

R.M.Van Wagoner, J.Clardy.

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.

Selected figure(s)

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.

Figures were selected by the author.