4cw4

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Crystal structure of the noncanonical ketosynthase FabY from P. aeruginosa

Structural highlights

4cw4 is a 1 chain structure with sequence from Pseudomonas aeruginosa PAO1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.349Å
Ligands:CL, SO4
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FABY_PSEAE Involved in the initiation of the fatty acid biosynthesis. Catalyzes the condensation of acetyl coenzyme A (acetyl-CoA) with malonyl-acyl carrier protein (ACP) to make the fatty acid synthesis (FAS) primer beta-acetoacetyl-ACP. It can also use short-chain acyl-CoA as substrates, including butyryl-CoA, and hexanoyl-CoA, but does not use any of the longer chain acyl-CoA substrates.[1] [2]

Publication Abstract from PubMed

Fungal fatty acid synthase (fFAS) is a key paradigm for the evolution of complex multienzymes. Its 48 functional domains are embedded in a matrix of scaffolding elements, which comprises almost 50% of the total sequence and determines the emergent multienzymes properties of fFAS. Catalytic domains of fFAS are derived from monofunctional bacterial enzymes, but the evolutionary origin of the scaffolding elements remains enigmatic. Here, we identify two bacterial protein families of noncanonical fatty acid biosynthesis starter enzymes and trans-acting polyketide enoyl reductases (ERs) as potential ancestors of scaffolding regions in fFAS. The architectures of both protein families are revealed by representative crystal structures of the starter enzyme FabY and DfnA-ER. In both families, a striking structural conservation of insertions to scaffolding elements in fFAS is observed, despite marginal sequence identity. The combined phylogenetic and structural data provide insights into the evolutionary origins of the complex multienzyme architecture of fFAS.

Evolutionary origins of the multienzyme architecture of giant fungal Fatty Acid synthase.,Bukhari HS, Jakob RP, Maier T Structure. 2014 Dec 2;22(12):1775-85. doi: 10.1016/j.str.2014.09.016. Epub 2014, Nov 13. PMID:25456814[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Citations
10 reviews cite this structure
Biosynthesis of polyketides by trans-AT polyketide synthases.
Helfrich et al. (2016)
9 more
9 other articles
No citations found

References

  1. ↑ Yuan Y, Sachdeva M, Leeds JA, Meredith TC. Fatty acid biosynthesis in Pseudomonas aeruginosa is initiated by the FabY class of beta-ketoacyl acyl carrier protein synthases. J Bacteriol. 2012 Oct;194(19):5171-84. doi: 10.1128/JB.00792-12. Epub 2012 Jun, 29. PMID:22753059 doi:http://dx.doi.org/10.1128/JB.00792-12
  2. ↑ Six DA, Yuan Y, Leeds JA, Meredith TC. Deletion of the beta-acetoacetyl synthase FabY in Pseudomonas aeruginosa induces hypoacylation of lipopolysaccharide and increases antimicrobial susceptibility. Antimicrob Agents Chemother. 2014;58(1):153-61. doi: 10.1128/AAC.01804-13. Epub, 2013 Oct 21. PMID:24145528 doi:http://dx.doi.org/10.1128/AAC.01804-13
  3. ↑ Bukhari HS, Jakob RP, Maier T. Evolutionary origins of the multienzyme architecture of giant fungal Fatty Acid synthase. Structure. 2014 Dec 2;22(12):1775-85. doi: 10.1016/j.str.2014.09.016. Epub 2014, Nov 13. PMID:25456814 doi:http://dx.doi.org/10.1016/j.str.2014.09.016

Contents


PDB ID 4cw4

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