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PDBsum entry 4ewp

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protein Protein-protein interface(s) links
Transferase PDB id
4ewp

 

 

 

 

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Contents
Protein chains
(+ 0 more) 349 a.a.
Waters ×877
PDB id:
4ewp
Name: Transferase
Title: Crystal structure of fabh from micrococcus luteus
Structure: 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
Source: 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
Resolution:
2.20Å     R-factor:   0.171     R-free:   0.210
Authors: J.H.Pereira,E.-B.Goh,J.D.Keasling,H.R.Beller,P.D.Adams
Key ref: 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: 22993086
Date:
27-Apr-12     Release date:   03-Oct-12    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
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)
Seq:
Struc:
350 a.a.
349 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.2.3.1.180  - beta-ketoacyl-[acyl-carrier-protein] synthase Iii.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: malonyl-[ACP] + acetyl-CoA + H+ = 3-oxobutanoyl-[ACP] + CO2 + CoA
malonyl-[ACP]
+ acetyl-CoA
+ H(+)
= 3-oxobutanoyl-[ACP]
+ CO2
+ CoA
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
Acta Crystallogr D Biol Crystallogr 68:1320-1328 (2012)
PubMed id: 22993086  
 
 
Structure of FabH and factors affecting the distribution of branched fatty acids in Micrococcus luteus.
J.H.Pereira, E.B.Goh, J.D.Keasling, H.R.Beller, P.D.Adams.
 
  ABSTRACT  
 
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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