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PDBsum entry 2afd

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protein links
Ligand binding protein PDB id
2afd
Jmol
Contents
Protein chain
88 a.a. *
* Residue conservation analysis
PDB id:
2afd
Name: Ligand binding protein
Title: Solution structure of asl1650, an acyl carrier protein from sp. Pcc 7120 with a variant phosphopantetheinylation-site s
Structure: Protein asl1650. Chain: a. Engineered: yes. Mutation: yes
Source: Nostoc sp.. Organism_taxid: 103690. Strain: pcc 7120. Expressed in: escherichia coli. Expression_system_taxid: 562. Other_details: synonym nostoc sp. Pcc 7120
NMR struc: 20 models
Authors: M.A.Johnson,W.Peti,T.Herrmann,I.A.Wilson,K.Wuthrich,Joint Ce Structural Genomics (Jcsg)
Key ref:
M.A.Johnson et al. (2006). Solution structure of Asl1650, an acyl carrier protein from Anabaena sp. PCC 7120 with a variant phosphopantetheinylation-site sequence. Protein Sci, 15, 1030-1041. PubMed id: 16597827 DOI: 10.1110/ps.051964606
Date:
25-Jul-05     Release date:   16-Aug-05    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q8YWG3  (Q8YWG3_NOSS1) -  Asl1650 protein
Seq:
Struc:
85 a.a.
88 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 

 
DOI no: 10.1110/ps.051964606 Protein Sci 15:1030-1041 (2006)
PubMed id: 16597827  
 
 
Solution structure of Asl1650, an acyl carrier protein from Anabaena sp. PCC 7120 with a variant phosphopantetheinylation-site sequence.
M.A.Johnson, W.Peti, T.Herrmann, I.A.Wilson, K.Wüthrich.
 
  ABSTRACT  
 
Cyanobacteria, such as Anabaena, produce a variety of bioactive natural products via polyketide synthases (PKS), nonribosomal peptide synthetases (NRPS), and hybrid peptide/polyketide pathways. The protein Asl1650, which is a member of the acyl carrier protein family from the cyanobacterium Anabaena sp. PCC 7120, is encoded in a region of the Anabaena genome that is rich in PKS and NRPS genes. To gain new insight into the physiological role of acyl carriers in Anabaena, the solution structure of Asl1650 has been solved by NMR spectroscopy. The protein adopts a twisted antiparallel four-helix bundle fold, with a variant phosphopantetheine-attachment motif positioned at the start of the second helix. Structure comparisons with proteins from other organisms suggest a likely physiological function as a discrete peptidyl carrier protein.
 
  Selected figure(s)  
 
Figure 2.
Wall-eye stereo views of the NMR structure of the protein Asl1650. (A) Bundle of 20 energy-minimized DYANA conformers. (Blue) Polypeptide backbone, (gold) hydrophobic side chains of the protein core. The positions of selected hydrophobic core residues are identified with the sequence numbers. (B) Ribbon diagram of the Asl1650 conformer with the lowest RMSD to the mean coordinates of the bundle of 20 conformers in panel A. The four helices forming a helix bundle (see text) are labeled [alpha]I, [alpha]II, 3[10](III), and [alpha]IV at their N termini. The chain-terminal residues [minus sign]3 and 85 are indicated.
Figure 4.
Wall-eye stereo view illustrating structural similarity in the region of the helix 3[10](III) between Asl1650 (blue) and TycC3 PCP (green). The backbone is represented by a spline function through the C^[alpha] positions, and the side chain heavy atoms are shown as stick diagrams. The orientation is such that side chains in the front right of the figure are exposed on the protein surface.
 
  The above figures are reprinted from an Open Access publication published by the Protein Society: Protein Sci (2006, 15, 1030-1041) copyright 2006.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
19636447 A.Koglin, and C.T.Walsh (2009).
Structural insights into nonribosomal peptide enzymatic assembly lines.
  Nat Prod Rep, 26, 987.  
18704089 A.Koglin, F.Löhr, F.Bernhard, V.V.Rogov, D.P.Frueh, E.R.Strieter, M.R.Mofid, P.Güntert, G.Wagner, C.T.Walsh, M.A.Marahiel, and V.Dötsch (2008).
Structural basis for the selectivity of the external thioesterase of the surfactin synthetase.
  Nature, 454, 907-911.
PDB code: 2k2q
18704088 D.P.Frueh, H.Arthanari, A.Koglin, D.A.Vosburg, A.E.Bennett, C.T.Walsh, and G.Wagner (2008).
Dynamic thiolation-thioesterase structure of a non-ribosomal peptide synthetase.
  Nature, 454, 903-906.
PDB code: 2roq
18770515 S.E.Evans, C.Williams, C.J.Arthur, S.G.Burston, T.J.Simpson, J.Crosby, and M.P.Crump (2008).
An ACP structural switch: conformational differences between the apo and holo forms of the actinorhodin polyketide synthase acyl carrier protein.
  Chembiochem, 9, 2424-2432.
PDB codes: 2k0x 2k0y
17653358 A.C.Mercer, and M.D.Burkart (2007).
The ubiquitous carrier protein--a window to metabolite biosynthesis.
  Nat Prod Rep, 24, 750-773.  
18059524 D.M.Byers, and H.Gong (2007).
Acyl carrier protein: structure-function relationships in a conserved multifunctional protein family.
  Biochem Cell Biol, 85, 649-662.  
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 code is shown on the right.