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PDBsum entry 4ewp
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PDB id:
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Transferase
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Title:
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Crystal structure of fabh from micrococcus luteus
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Structure:
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3-oxoacyl-[acyl-carrier-protein] synthase 3. Chain: a, b, c, d, e, f. Synonym: 3-oxoacyl-[acyl-carrier-protein] synthase iii, beta- ketoacyl-acp synthase iii. Engineered: yes
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Source:
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Micrococcus luteus nctc 2665. Organism_taxid: 465515. Strain: atcc 4698 / dsm 20030 / jcm 1464 / nbrc 3333 / ncimb 9278 / nctc 2665 / vkm ac-2230. Gene: fabh, hmpref0569_0014, mlut_09310. Expressed in: escherichia coli. Expression_system_taxid: 562
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Resolution:
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2.20Å
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R-factor:
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0.171
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R-free:
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0.210
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Authors:
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J.H.Pereira,E.-B.Goh,J.D.Keasling,H.R.Beller,P.D.Adams
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Key ref:
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J.H.Pereira
et al.
(2012).
Structure of FabH and factors affecting the distribution of branched fatty acids in Micrococcus luteus.
Acta Crystallogr D Biol Crystallogr,
68,
1320-1328.
PubMed id:
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Date:
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27-Apr-12
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Release date:
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03-Oct-12
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PROCHECK
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Headers
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References
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C5CAR9
(C5CAR9_MICLC) -
Beta-ketoacyl-[acyl-carrier-protein] synthase III from Micrococcus luteus (strain ATCC 4698 / DSM 20030 / JCM 1464 / NBRC 3333 / NCIMB 9278 / NCTC 2665 / VKM Ac-2230)
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Seq: Struc:
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350 a.a.
349 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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Enzyme class:
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E.C.2.3.1.180
- beta-ketoacyl-[acyl-carrier-protein] synthase Iii.
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Reaction:
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malonyl-[ACP] + acetyl-CoA + H+ = 3-oxobutanoyl-[ACP] + CO2 + CoA
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malonyl-[ACP]
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acetyl-CoA
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+
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H(+)
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=
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3-oxobutanoyl-[ACP]
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+
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CO2
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+
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CoA
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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Acta Crystallogr D Biol Crystallogr
68:1320-1328
(2012)
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PubMed id:
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Structure of FabH and factors affecting the distribution of branched fatty acids in Micrococcus luteus.
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J.H.Pereira,
E.B.Goh,
J.D.Keasling,
H.R.Beller,
P.D.Adams.
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ABSTRACT
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Micrococcus luteus is a Gram-positive bacterium that produces iso- and
anteiso-branched alkenes by the head-to-head condensation of fatty-acid
thioesters [coenzyme A (CoA) or acyl carrier protein (ACP)]; this activity is of
interest for the production of advanced biofuels. In an effort to better
understand the control of the formation of branched fatty acids in M. luteus,
the structure of FabH (MlFabH) was determined. FabH, or β-ketoacyl-ACP synthase
III, catalyzes the initial step of fatty-acid biosynthesis: the condensation of
malonyl-ACP with an acyl-CoA. Analysis of the MlFabH structure provides insights
into its substrate selectivity with regard to length and branching of the
acyl-CoA. The most structurally divergent region of FabH is the L9 loop region
located at the dimer interface, which is involved in the formation of the
acyl-binding channel and thus limits the substrate-channel size. The residue
Phe336, which is positioned near the catalytic triad, appears to play a major
role in branched-substrate selectivity. In addition to structural studies of
MlFabH, transcriptional studies of M. luteus were also performed, focusing on
the increase in the ratio of anteiso:iso-branched alkenes that was observed
during the transition from early to late stationary phase. Gene-expression
microarray analysis identified two genes involved in leucine and isoleucine
metabolism that may explain this transition.
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}
}
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