4FQ9: Crystal Structure Of 3-hydroxydecanoyl-acyl Carrier Protein Dehydratase (faba) From Pseudomonas Aeruginosa

Fatty acid biosynthesis is an essential component of metabolism in both eukaryotes and prokaryotes. The fatty acid biosynthetic pathway of Gram-negative bacteria is an established therapeutic target. Two homologous enzymes FabA and FabZ catalyze a key step in fatty acid biosynthesis; both dehydrate hydroxyacyl fatty acids that are coupled via a phosphopantetheine to an acyl carrier protein (ACP). The resulting trans-2-enoyl-ACP is further polymerized in a processive manner. FabA, however, carries out a second reaction involving isomerization of trans-2-enoyl fatty acid to cis-3-enoyl fatty acid. We have solved the structure of Pseudomonas aeruginosa FabA with a substrate allowing detailed molecular insight into the interactions of the active site. This has allowed a detailed examination of the factors governing the second catalytic step. We have also determined the structure of FabA in complex with small molecules (so-called fragments). These small molecules occupy distinct regions of the active site and form the basis for a rational inhibitor design program.
PDB ID: 4FQ9Download
MMDB ID: 108651
PDB Deposition Date: 2012/6/25
Updated in MMDB: 2013/03
Experimental Method:
x-ray diffraction
Resolution: 2.02  Å
Source Organism:
Similar Structures:
Biological Unit for 4FQ9: dimeric; determined by author and by software (PISA)
Molecular Components in 4FQ9
Label Count Molecule
Proteins (2 molecules)
3-hydroxydecanoyl-[acyl-carrier-protein] Dehydratase(Gene symbol: fabA)
Molecule annotation
Chemicals (4 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB