PDBsum entry: 3il4

Transferase

PDB-id: 3il4

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References

PROCHECK

Protein chains

318 a.a. *

Ligands

ACO ×4

Waters ×45

* Residue conservation analysis

Tools

Clefts Calculation

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PDB id:

3il4

Name:

Transferase

Title:

Structure of e. Faecalis fabh in complex with acetyl coa

Structure:

3-oxoacyl-[acyl-carrier-protein] synthase 3. Chain: a, b, c, d. Synonym: 3-oxoacyl-[acyl-carrier-protein] synthase iii, beta-ketoacyl-acp synthase iii, kas iii. Engineered: yes. Mutation: yes

Source:

Enterococcus faecalis. Organism_taxid: 1351. Gene: ef_2885, fabh. Expressed in: escherichia coli. Expression_system_taxid: 562

UniProt:

Chains A, B, C, D: Q820T1 (FABH_ENTFA)

Seq:

Struc:

Seq:

321 a.a.

Struc:

318 a.a.*

Key:

PfamA domain

Secondary structure

* PDB and UniProt seqs differ at 4 residue positions (black crosses)

Enzyme class:

E.C.2.3.1.180   [IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

Reaction:

Acetyl-CoA + malonyl-[acyl-carrier-protein] = acetoacyl-[acyl-carrier- protein] + CoA + CO₂

Resolution:

3.00Å

R-factor:

0.196

R-free:

0.270

Authors:

K.S.Gajiwala,S Margosiak,J.Lu,J.Cortez,Y.Su,Z.Nie,K.Appelt

Key ref:

K.S.Gajiwala et al. (2009). Crystal structures of bacterial FabH suggest a molecular basis for the substrate specificity of the enzyme.. FEBS Lett, 583, 2939-2946. [PubMed id: 19665020] [DOI: 10.1016/j.febslet.2009.08.001]

Date:

06-Aug-09

Release date:

25-Aug-09

Related entries:

3il3
structure of haemophilus influenzae fabh
3il5
structure of e. Faecalis fabh in complex with 2-({4-bromo-
3-[(diethylamino)sulfonyl]benzoyl}amino)benzoic acid
3il6
structure of e. Faecalis fabh in complex with 2-({4-[(3r,
5s)-3,5-dimethylpiperidin-1-yl]-3-phenoxybenzoyl}amino)
benzoic acid
3il7
... plus others (see Header records)

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Surface

Key reference

DOI no: 10.1016/j.febslet.2009.08.001

FEBS Lett 583:2939-2946 (2009)

PubMed id: 19665020

Crystal structures of bacterial FabH suggest a molecular basis for the substrate specificity of the enzyme.

K.S.Gajiwala, S.Margosiak, J.Lu, J.Cortez, Y.Su, Z.Nie, K.Appelt.

ABSTRACT

FabH (beta-ketoacyl-acyl carrier protein synthase III) is unique in that it initiates fatty acid biosynthesis, is inhibited by long-chain fatty acids providing means for feedback control of the process, and dictates the fatty acid profile of the organism by virtue of its substrate specificity. We report the crystal structures of bacterial FabH enzymes from four different pathogenic species: Enterococcus faecalis, Haemophilus influenzae, Staphylococcus aureus and Escherichia coli. Structural data on the enzyme from different species show important differences in the architecture of the substrate-binding sites that parallel the inter-species diversity in the substrate specificities of these enzymes.