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* Residue conservation analysis
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PDB id:
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Transferase
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Title:
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Structure of e. Faecalis fabh in complex with 2-({4-bromo-3- [(diethylamino)sulfonyl]benzoyl}amino)benzoic acid
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Structure:
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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
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Source:
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Enterococcus faecalis. Organism_taxid: 1351. Gene: ef_2885, fabh. Expressed in: escherichia coli. Expression_system_taxid: 562
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Resolution:
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2.60Å
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R-factor:
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0.189
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R-free:
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0.260
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Authors:
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K.S.Gajiwala,S Margosiak,J.Lu,J.Cortez,Y.Su,Z.Nie,K.Appelt
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Key ref:
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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:
DOI:
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Date:
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06-Aug-09
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Release date:
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25-Aug-09
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PROCHECK
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Headers
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References
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Q820T1
(FABH_ENTFA) -
3-oxoacyl-[acyl-carrier-protein] synthase 3
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Seq:
Struc:
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321 a.a.
320 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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Acetyl-CoA + malonyl-[acyl-carrier-protein] = acetoacetyl-[acyl-carrier- protein] + CoA + CO2
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Acetyl-CoA
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+
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malonyl-[acyl-carrier-protein]
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=
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acetoacetyl-[acyl-carrier- protein]
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+
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CoA
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+
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CO(2)
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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Gene Ontology (GO) functional annotation
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Cellular component
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cytoplasm
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1 term
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Biological process
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metabolic process
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3 terms
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Biochemical function
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catalytic activity
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6 terms
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DOI no:
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Febs Lett
583:2939-2946
(2009)
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PubMed id:
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Crystal structures of bacterial FabH suggest a molecular basis for the substrate specificity of the enzyme.
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K.S.Gajiwala,
S.Margosiak,
J.Lu,
J.Cortez,
Y.Su,
Z.Nie,
K.Appelt.
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ABSTRACT
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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.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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Y.Pérez-Castillo,
M.Froeyen,
M.A.Cabrera-Pérez,
and
A.Nowé
(2011).
Molecular dynamics and docking simulations as a proof of high flexibility in E. coli FabH and its relevance for accurate inhibitor modeling.
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J Comput Aided Mol Des, 25,
371-393.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
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Links
