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PDBsum entry 1i01

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protein Protein-protein interface(s) links
Oxidoreductase PDB id
1i01
Jmol
Contents
Protein chains
228 a.a. *
(+ 0 more) 231 a.a. *
Waters ×349
* Residue conservation analysis
PDB id:
1i01
Name: Oxidoreductase
Title: Crystal structure of beta-ketoacyl [acyl carrier protein] reductase from e. Coli.
Structure: Beta-ketoacyl [acp] reductase. Chain: a, b, c, d, e, f, g, h. Synonym: 3-oxoacyl-[acyl-carrier protein] reductase, 3- ketoacyl-acyl carrier protein reductase. Engineered: yes
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562
Biol. unit: Tetramer (from PQS)
Resolution:
2.60Å     R-factor:   0.228     R-free:   0.250
Authors: A.C.Price,C.O.Rock,S.W.White
Key ref:
A.C.Price et al. (2001). Structure of beta-ketoacyl-[acyl carrier protein] reductase from Escherichia coli: negative cooperativity and its structural basis. Biochemistry, 40, 12772-12781. PubMed id: 11669613 DOI: 10.1021/bi010737g
Date:
27-Jan-01     Release date:   07-Feb-01    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P0AEK2  (FABG_ECOLI) -  3-oxoacyl-[acyl-carrier-protein] reductase FabG
Seq:
Struc:
244 a.a.
228 a.a.
Protein chains
Pfam   ArchSchema ?
P0AEK2  (FABG_ECOLI) -  3-oxoacyl-[acyl-carrier-protein] reductase FabG
Seq:
Struc:
244 a.a.
231 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: Chains A, B, C, D, E, F, G, H: E.C.1.1.1.100  - 3-oxoacyl-[acyl-carrier-protein] reductase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: (3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP+ = 3-oxoacyl-[acyl- carrier-protein] + NADPH
(3R)-3-hydroxyacyl-[acyl-carrier-protein]
+ NADP(+)
= 3-oxoacyl-[acyl- carrier-protein]
+ NADPH
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     metabolic process   8 terms 
  Biochemical function     oxidoreductase activity     6 terms  

 

 
    reference    
 
 
DOI no: 10.1021/bi010737g Biochemistry 40:12772-12781 (2001)
PubMed id: 11669613  
 
 
Structure of beta-ketoacyl-[acyl carrier protein] reductase from Escherichia coli: negative cooperativity and its structural basis.
A.C.Price, Y.M.Zhang, C.O.Rock, S.W.White.
 
  ABSTRACT  
 
The structure of beta-ketoacyl-[acyl carrier protein] reductase (FabG) from Escherichia coli was determined via the multiwavelength anomalous diffraction technique using a selenomethionine-labeled crystal containing 88 selenium sites in the asymmetric unit. The comparison of the E. coli FabG structure with the homologous Brassica napus FabG.NADP(+) binary complex reveals that cofactor binding causes a substantial conformational change in the protein. This conformational change puts all three active-site residues (Ser 138, Tyr 151, and Lys 155) into their active configurations and provides a structural mechanism for allosteric communication between the active sites in the homotetramer. FabG exhibits negative cooperative binding of NADPH, and this effect is enhanced by the presence of acyl carrier protein (ACP). NADPH binding also increases the affinity and decreases the maximum binding of ACP to FabG. Thus, unlike other members of the short-chain dehydrogenase/reductase superfamily, FabG undergoes a substantial conformational change upon cofactor binding that organizes the active-site triad and alters the affinity of the other substrate-binding sites in the tetrameric enzyme.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
19444866 D.Wu, X.D.Wu, X.F.You, X.F.Ma, and W.X.Tian (2010).
Inhibitory effects on bacterial growth and beta-ketoacyl-ACP reductase by different species of maple leaf extracts and tannic acid.
  Phytother Res, 24, S35-S41.  
20731893 T.Maier, M.Leibundgut, D.Boehringer, and N.Ban (2010).
Structure and function of eukaryotic fatty acid synthases.
  Q Rev Biophys, 43, 373-422.  
19746209 A.Gurvitz (2009).
Caenorhabditis elegans F09E10.3 encodes a putative 3-oxoacyl-thioester reductase of mitochondrial type 2 fatty acid synthase FASII that is functional in yeast.
  J Biomed Biotechnol, 2009, 235868.  
  20145708 A.Gurvitz (2009).
Identification of the Leishmania major proteins LmjF07.0430, LmjF07.0440, and LmjF27.2440 as components of fatty acid synthase II.
  J Biomed Biotechnol, 2009, 950864.  
19648370 J.Han, Q.Lu, L.Zhou, H.Liu, and H.Xiang (2009).
Identification of the polyhydroxyalkanoate (PHA)-specific acetoacetyl coenzyme A reductase among multiple FabG paralogs in Haloarcula hispanica and reconstruction of the PHA biosynthetic pathway in Haloferax volcanii.
  Appl Environ Microbiol, 75, 6168-6175.  
19550039 M.J.Li, A.Q.Li, H.Xia, C.Z.Zhao, C.S.Li, S.B.Wan, Y.P.Bi, and X.J.Wang (2009).
Cloning and sequence analysis of putative type II fatty acid synthase genes from Arachis hypogaea L.
  J Biosci, 34, 227-238.  
19362634 S.C.Tsai, and B.D.Ames (2009).
Structural enzymology of polyketide synthases.
  Methods Enzymol, 459, 17-47.  
18611377 D.J.Miller, A.Jerga, C.O.Rock, and S.W.White (2008).
Analysis of the Staphylococcus aureus DgkB structure reveals a common catalytic mechanism for the soluble diacylglycerol kinases.
  Structure, 16, 1036-1046.
PDB codes: 2qv7 2qvl
18791006 K.Hölsch, J.Havel, M.Haslbeck, and D.Weuster-Botz (2008).
Identification, cloning, and characterization of a novel ketoreductase from the cyanobacterium Synechococcus sp. strain PCC 7942.
  Appl Environ Microbiol, 74, 6697-6702.  
17879351 K.Karmodiya, and N.Surolia (2008).
A unique and differential effect of denaturants on cofactor mediated activation of Plasmodium falciparum beta-ketoacyl-ACP reductase.
  Proteins, 70, 528-538.  
18721141 K.Karmodiya, R.Modak, N.Sahoo, S.Sajad, and N.Surolia (2008).
Deciphering the key residues in Plasmodium falciparum beta-ketoacyl acyl carrier protein reductase responsible for interactions with Plasmodium falciparum acyl carrier protein.
  FEBS J, 275, 4756-4766.  
17894349 N.R.Zaccai, L.G.Carter, N.S.Berrow, S.Sainsbury, J.E.Nettleship, T.S.Walter, K.Harlos, R.J.Owens, K.S.Wilson, D.I.Stuart, and R.M.Esnouf (2008).
Crystal structure of a 3-oxoacyl-(acylcarrier protein) reductase (BA3989) from Bacillus anthracis at 2.4-A resolution.
  Proteins, 70, 562-567.
PDB code: 2uvd
18566346 R.Zhang, G.Zhu, W.Zhang, S.Cao, X.Ou, X.Li, M.Bartlam, Y.Xu, X.C.Zhang, and Z.Rao (2008).
Crystal structure of a carbonyl reductase from Candida parapsilosis with anti-Prelog stereospecificity.
  Protein Sci, 17, 1412-1423.
PDB code: 3ctm
17242430 C.E.Christensen, B.B.Kragelund, P.von Wettstein-Knowles, and A.Henriksen (2007).
Structure of the human beta-ketoacyl [ACP] synthase from the mitochondrial type II fatty acid synthase.
  Protein Sci, 16, 261-272.
PDB codes: 2iwy 2iwz 2ix4
17642518 G.Poncet-Montange, S.Ducasse-Cabanot, A.Quemard, G.Labesse, and M.Cohen-Gonsaud (2007).
Lack of dynamics in the MabA active site kills the enzyme activity: practical consequences for drug-design studies.
  Acta Crystallogr D Biol Crystallogr, 63, 923-925.
PDB code: 2ntn
17958702 K.S.Paithankar, C.Feller, E.B.Kuettner, A.Keim, M.Grunow, and N.Sträter (2007).
Cosubstrate-induced dynamics of D-3-hydroxybutyrate dehydrogenase from Pseudomonas putida.
  FEBS J, 274, 5767-5779.
PDB codes: 2q2q 2q2v 2q2w
  17277451 Q.Mao, W.L.Duax, and T.C.Umland (2007).
Crystallization and X-ray diffraction analysis of the beta-ketoacyl-acyl carrier protein reductase FabG from Aquifex aeolicus VF5.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 63, 106-109.  
17431175 S.Jenni, M.Leibundgut, D.Boehringer, C.Frick, B.Mikolásek, and N.Ban (2007).
Structure of fungal fatty acid synthase and implications for iterative substrate shuttling.
  Science, 316, 254-261.
PDB codes: 2uv9 2uva 2uvb 2uvc
17898897 S.Smith, and S.C.Tsai (2007).
The type I fatty acid and polyketide synthases: a tale of two megasynthases.
  Nat Prod Rep, 24, 1041-1072.  
17167539 B.H.Li, R.Zhang, Y.T.Du, Y.H.Sun, and W.X.Tian (2006).
Inactivation mechanism of the beta-ketoacyl-[acyl carrier protein] reductase of bacterial type-II fatty acid synthase by epigallocatechin gallate.
  Biochem Cell Biol, 84, 755-762.  
16540431 B.H.Li, X.F.Ma, X.D.Wu, and W.X.Tian (2006).
Inhibitory activity of chlorogenic acid on enzymes involved in the fatty acid synthesis in animals and bacteria.
  IUBMB Life, 58, 39-46.  
16624803 D.J.Miller, Y.M.Zhang, C.O.Rock, and S.W.White (2006).
Structure of RhlG, an essential beta-ketoacyl reductase in the rhamnolipid biosynthetic pathway of Pseudomonas aeruginosa.
  J Biol Chem, 281, 18025-18032.
PDB code: 2b4q
16245348 D.Xie, Z.Shao, J.Achkar, W.Zha, J.W.Frost, and H.Zhao (2006).
Microbial synthesis of triacetic acid lactone.
  Biotechnol Bioeng, 93, 727-736.  
16934037 K.Karmodiya, and N.Surolia (2006).
Analyses of co-operative transitions in Plasmodium falciparum beta-ketoacyl acyl carrier protein reductase upon co-factor and acyl carrier protein binding.
  FEBS J, 273, 4093-4103.  
16513975 T.Maier, S.Jenni, and N.Ban (2006).
Architecture of mammalian fatty acid synthase at 4.5 A resolution.
  Science, 311, 1258-1262.
PDB code: 2cf2
16085817 C.T.Nomura, K.Taguchi, Z.Gan, K.Kuwabara, T.Tanaka, K.Takase, and Y.Doi (2005).
Expression of 3-ketoacyl-acyl carrier protein reductase (fabG) genes enhances production of polyhydroxyalkanoate copolymer from glucose in recombinant Escherichia coli JM109.
  Appl Environ Microbiol, 71, 4297-4306.  
15513927 D.J.Hosfield, Y.Wu, R.J.Skene, M.Hilgers, A.Jennings, G.P.Snell, and K.Aertgeerts (2005).
Conformational flexibility in crystal structures of human 11beta-hydroxysteroid dehydrogenase type I provide insights into glucocorticoid interconversion and enzyme regulation.
  J Biol Chem, 280, 4639-4648.
PDB codes: 1xu7 1xu9
15970585 E.K.Bomati, M.B.Austin, M.E.Bowman, R.A.Dixon, and J.P.Noel (2005).
Structural elucidation of chalcone reductase and implications for deoxychalcone biosynthesis.
  J Biol Chem, 280, 30496-30503.
PDB code: 1zgd
16332089 J.Wu, T.J.Zaleski, C.Valenzano, C.Khosla, and D.E.Cane (2005).
Polyketide double bond biosynthesis. Mechanistic analysis of the dehydratase-containing module 2 of the picromycin/methymycin polyketide synthase.
  J Am Chem Soc, 127, 17393-17404.  
15977159 M.Cohen-Gonsaud, S.Ducasse-Cabanot, A.Quemard, and G.Labesse (2005).
Ligand-induced fit in mycobacterial MabA: the sequence-specific C-terminus locks the conformational change.
  Proteins, 60, 392-400.  
15952903 S.W.White, J.Zheng, Y.M.Zhang, and Rock (2005).
The structural biology of type II fatty acid biosynthesis.
  Annu Rev Biochem, 74, 791-831.  
15987605 Y.M.Qin, F.M.Pujol, Y.H.Shi, J.X.Feng, Y.M.Liu, A.J.Kastaniotis, J.K.Hiltunen, and Y.X.Zhu (2005).
Cloning and functional characterization of two cDNAs encoding NADPH-dependent 3-ketoacyl-CoA reductased from developing cotton fibers.
  Cell Res, 15, 465-473.  
15016358 A.C.Price, Y.M.Zhang, C.O.Rock, and S.W.White (2004).
Cofactor-induced conformational rearrangements establish a catalytically competent active site and a proton relay conduit in FabG.
  Structure, 12, 417-428.
PDB codes: 1q7b 1q7c
14996818 C.Y.Lai, and J.E.Cronan (2004).
Isolation and characterization of beta-ketoacyl-acyl carrier protein reductase (fabG) mutants of Escherichia coli and Salmonella enterica serovar Typhimurium.
  J Bacteriol, 186, 1869-1878.  
15371447 M.S.Kimber, F.Martin, Y.Lu, S.Houston, M.Vedadi, A.Dharamsi, K.M.Fiebig, M.Schmid, and C.O.Rock (2004).
The structure of (3R)-hydroxyacyl-acyl carrier protein dehydratase (FabZ) from Pseudomonas aeruginosa.
  J Biol Chem, 279, 52593-52602.
PDB code: 1u1z
  15043388 R.J.Heath, and C.O.Rock (2004).
Fatty acid biosynthesis as a target for novel antibacterials.
  Curr Opin Investig Drugs, 5, 146-153.  
15544323 T.P.Korman, J.A.Hill, T.N.Vu, and S.C.Tsai (2004).
Structural analysis of actinorhodin polyketide ketoreductase: cofactor binding and substrate specificity.
  Biochemistry, 43, 14529-14538.
PDB codes: 1x7g 1x7h 1xr3
15726819 Y.M.Zhang, Y.J.Lu, and C.O.Rock (2004).
The reductase steps of the type II fatty acid synthase as antimicrobial targets.
  Lipids, 39, 1055-1060.  
12897013 H.Wang, and J.E.Cronan (2003).
Haemophilus influenzae Rd lacks a stringently conserved fatty acid biosynthetic enzyme and thermal control of membrane lipid composition.
  J Bacteriol, 185, 4930-4937.  
12499205 R.F.Waller, S.A.Ralph, M.B.Reed, V.Su, J.D.Douglas, D.E.Minnikin, A.F.Cowman, G.S.Besra, and G.I.McFadden (2003).
A type II pathway for fatty acid biosynthesis presents drug targets in Plasmodium falciparum.
  Antimicrob Agents Chemother, 47, 297-301.  
12689621 S.Smith, A.Witkowski, and A.K.Joshi (2003).
Structural and functional organization of the animal fatty acid synthase.
  Prog Lipid Res, 42, 289-317.  
14527946 Y.M.Zhang, B.Wu, J.Zheng, and C.O.Rock (2003).
Key residues responsible for acyl carrier protein and beta-ketoacyl-acyl carrier protein reductase (FabG) interaction.
  J Biol Chem, 278, 52935-52943.  
12237320 H.Marrakchi, K.H.Choi, and C.O.Rock (2002).
A new mechanism for anaerobic unsaturated fatty acid formation in Streptococcus pneumoniae.
  J Biol Chem, 277, 44809-44816.  
12501157 R.L.Rich, and D.G.Myszka (2002).
Survey of the year 2001 commercial optical biosensor literature.
  J Mol Recognit, 15, 352-376.  
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. Where a reference describes a PDB structure, the PDB codes are shown on the right.