PDBsum entry 2k92

Go to PDB code: 
protein links
Lipid transport PDB id
Protein chain
77 a.a. *
* Residue conservation analysis
PDB id:
Name: Lipid transport
Title: Structural modification of acyl carrier protein by butyryl group
Structure: Acyl carrier protein. Chain: a. Synonym: acp, cytosolic-activating factor, caf, fatty acid synthase acyl carrier protein. Engineered: yes. Other_details: apo form
Source: Escherichia coli. Organism_taxid: 562. Gene: acpp, b1094, jw1080. Expressed in: escherichia coli. Expression_system_taxid: 562.
NMR struc: 20 models
Authors: B.N.Wu
Key ref:
B.N.Wu et al. (2009). Structural modification of acyl carrier protein by butyryl group. Protein Sci, 18, 240-246. PubMed id: 19177367 DOI: 10.1002/pro.11
29-Sep-08     Release date:   20-Jan-09    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P0A6A8  (ACP_ECOLI) -  Acyl carrier protein
78 a.a.
77 a.a.*
Key:    PfamA domain  Secondary structure
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   1 term 
  Biological process     lipid metabolic process   6 terms 
  Biochemical function     acyl binding     4 terms  


DOI no: 10.1002/pro.11 Protein Sci 18:240-246 (2009)
PubMed id: 19177367  
Structural modification of acyl carrier protein by butyryl group.
B.N.Wu, Y.M.Zhang, C.O.Rock, J.J.Zheng.
Fatty acid synthesis in bacteria is catalyzed by a set of individual enzymes known as the type II fatty acid synthase. Acyl carrier protein (ACP) shuttles the acyl intermediates between individual pathway enzymes. In this study, we determined the solution structures of three different forms of ACP, apo-ACP, ACP, and butyryl-ACP under identical experimental conditions. The structural studies revealed that attachment of butyryl acyl intermediate to ACP alters the conformation of ACP. This finding supports the more general notion that the attachment of different acyl intermediates alters the ACP structure to facilitate their recognition and turnover by the appropriate target enzymes.
  Selected figure(s)  
Figure 1.
Solution strucures of ACPs. Stereo view of the ensemble of the 20 best structures of apo-ACP (A), ACP (B), and C4:0-ACP (C). Helices I --IV are shown in red, green, orange, and purple, respectively.
Figure 2.
Comparisons of the structures of different forms of ACP. (A) Superposition of the solution (blue) and crystal (gray) structures of C4-0-ACP. (B) The representative structures of apo-ACP (red) and ACP (green) are superimposed by fitting the backbone atoms of the three long helices (residues 4 --15, 36 --50, and 66 --74). The four helices are labeled by Roman numerals and the location of Ser36 is indicated by a red arrow. (C) The representative structures of C4:0-ACP (blue) and ACP (green) were superimposed. The movement of loop II/helix III was circled in cyan. (D) Hydrophobicity of each residue is calculated based on Kyte --Doolittle-hydrophobicity value23 and then visualized on the surface map of solution structure of C4:0-ACP using Chimera program.24 The hydrophobic residues are colored in green, the neutral residues are colored in gray, and the hydrophilic residues are colored in cyan. Three residues in helix II are pointed by black arrow, and helix III is labeled on the surface.
  The above figures are reprinted from an Open Access publication published by the Protein Society: Protein Sci (2009, 18, 240-246) copyright 2009.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20659690 E.Płoskoń, C.J.Arthur, A.L.Kanari, P.Wattana-amorn, C.Williams, J.Crosby, T.J.Simpson, C.L.Willis, and M.P.Crump (2010).
Recognition of intermediate functionality by acyl carrier protein over a complete cycle of fatty acid biosynthesis.
  Chem Biol, 17, 776-785.
PDB codes: 2koo 2kop 2koq 2kor 2kos
20083605 G.Volkmann, P.W.Murphy, E.E.Rowland, J.E.Cronan, X.Q.Liu, C.Blouin, and D.M.Byers (2010).
Intein-mediated cyclization of bacterial acyl carrier protein stabilizes its folded conformation but does not abolish function.
  J Biol Chem, 285, 8605-8614.  
  19768685 J.R.Gallagher, and S.T.Prigge (2010).
Plasmodium falciparum acyl carrier protein crystal structures in disulfide-linked and reduced states and their prevalence during blood stage growth.
  Proteins, 78, 575-588.
PDB codes: 3gzl 3gzm
20659683 L.Tran, R.W.Broadhurst, M.Tosin, A.Cavalli, and K.J.Weissman (2010).
Insights into protein-protein and enzyme-substrate interactions in modular polyketide synthases.
  Chem Biol, 17, 705-716.  
21070944 M.Babu, J.F.Greenblatt, A.Emili, N.C.Strynadka, R.A.Reithmeier, and T.F.Moraes (2010).
Structure of a SLC26 anion transporter STAS domain in complex with acyl carrier protein: implications for E. coli YchM in fatty acid metabolism.
  Structure, 18, 1450-1462.
PDB code: 3ny7
20551137 P.Carbonell, and J.L.Faulon (2010).
Molecular signatures-based prediction of enzyme promiscuity.
  Bioinformatics, 26, 2012-2019.  
20182923 S.K.Upadhyay, A.Misra, N.Surolia, A.Surolia, and M.Sundd (2010).
Backbone chemical shift assignments of the acyl-acyl carrier protein intermediates of the fatty acid biosynthesis pathway of Plasmodium falciparum.
  Biomol NMR Assign, 4, 83-85.  
19636447 A.Koglin, and C.T.Walsh (2009).
Structural insights into nonribosomal peptide enzymatic assembly lines.
  Nat Prod Rep, 26, 987.  
19520851 S.K.Upadhyay, A.Misra, R.Srivastava, N.Surolia, A.Surolia, and M.Sundd (2009).
Structural insights into the acyl intermediates of the Plasmodium falciparum fatty acid synthesis pathway: the mechanism of expansion of the acyl carrier protein core.
  J Biol Chem, 284, 22390-22400.  
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.