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PDBsum entry 3f09

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protein Protein-protein interface(s) links
Transferase PDB id
3f09
Jmol
Contents
Protein chains
122 a.a. *
116 a.a. *
122 a.a. *
Waters ×314
* Residue conservation analysis
Superseded by: 4jm7
PDB id:
3f09
Name: Transferase
Title: 1.82 angstrom resolution crystal structure of holo-(acyl-car protein) synthase (acps) from staphylococcus aureus
Structure: Holo-[acyl-carrier-protein] synthase. Chain: a, b, c. Synonym: holo-acp synthase, 4'-phosphopantetheinyl transfer engineered: yes
Source: Staphylococcus aureus subsp. Aureus co organism_taxid: 93062. Strain: staphylococcus aureus subsp. Aureus col. Gene: acps, sacol2061. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.82Å     R-factor:   0.192     R-free:   0.232
Authors: A.S.Halavaty,G.Minasov,L.Shuvalova,I.Dubrovska,L.Papazisi, W.F.Anderson,Center For Structural Genomics Of Infectious D (Csgid)
Key ref: A.S.Halavaty et al. (2012). Structural characterization and comparison of three acyl-carrier-protein synthases from pathogenic bacteria. Acta Crystallogr D Biol Crystallogr, 68, 1359-1370. PubMed id: 22993090
Date:
24-Oct-08     Release date:   11-Nov-08    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q5HED0  (ACPS_STAAC) -  Holo-[acyl-carrier-protein] synthase
Seq:
Struc:
119 a.a.
122 a.a.
Protein chain
Pfam   ArchSchema ?
Q5HED0  (ACPS_STAAC) -  Holo-[acyl-carrier-protein] synthase
Seq:
Struc:
119 a.a.
116 a.a.
Protein chain
Pfam   ArchSchema ?
Q5HED0  (ACPS_STAAC) -  Holo-[acyl-carrier-protein] synthase
Seq:
Struc:
119 a.a.
122 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: Chain A: E.C.2.7.8.7  - Holo-[acyl-carrier-protein] synthase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: CoA-(4'-phosphopantetheine) + apo-[acyl-carrier-protein] = adenosine 3',5'-bisphosphate + holo-[acyl-carrier-protein]
CoA-(4'-phosphopantetheine)
+ apo-[acyl-carrier-protein]
= adenosine 3',5'-bisphosphate
+ holo-[acyl-carrier-protein]
      Cofactor: Mg(2+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    Added reference    
 
 
Acta Crystallogr D Biol Crystallogr 68:1359-1370 (2012)
PubMed id: 22993090  
 
 
Structural characterization and comparison of three acyl-carrier-protein synthases from pathogenic bacteria.
A.S.Halavaty, Y.Kim, G.Minasov, L.Shuvalova, I.Dubrovska, J.Winsor, M.Zhou, O.Onopriyenko, T.Skarina, L.Papazisi, K.Kwon, S.N.Peterson, A.Joachimiak, A.Savchenko, W.F.Anderson.
 
  ABSTRACT  
 
Some bacterial type II fatty-acid synthesis (FAS II) enzymes have been shown to be important candidates for drug discovery. The scientific and medical quest for new FAS II protein targets continues to stimulate research in this field. One of the possible additional candidates is the acyl-carrier-protein synthase (AcpS) enzyme. Its holo form post-translationally modifies the apo form of an acyl carrier protein (ACP), which assures the constant delivery of thioester intermediates to the discrete enzymes of FAS II. At the Center for Structural Genomics of Infectious Diseases (CSGID), AcpSs from Staphylococcus aureus (AcpS(SA)), Vibrio cholerae (AcpS(VC)) and Bacillus anthracis (AcpS(BA)) have been structurally characterized in their apo, holo and product-bound forms, respectively. The structure of AcpS(BA) is emphasized because of the two 3',5'-adenosine diphosphate (3',5'-ADP) product molecules that are found in each of the three coenzyme A (CoA) binding sites of the trimeric protein. One 3',5'-ADP is bound as the 3',5'-ADP part of CoA in the known structures of the CoA-AcpS and 3',5'-ADP-AcpS binary complexes. The position of the second 3',5'-ADP has never been described before. It is in close proximity to the first 3',5'-ADP and the ACP-binding site. The coordination of two ADPs in AcpS(BA) may possibly be exploited for the design of AcpS inhibitors that can block binding of both CoA and ACP.