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Literature summary extracted from

  • Jung, J.; Bashiri, G.; Johnston, J.M.; Brown, A.S.; Ackerley, D.F.; Baker, E.N.
    Crystal structure of the essential Mycobacterium tuberculosis phosphopantetheinyl transferase PptT, solved as a fusion protein with maltose binding protein (2014), J. Struct. Biol., 188, 274-278.
    View publication on PubMed

Application

EC Number Application Comment Organism
2.7.8.7 drug development the human pathogen Mycobacterium tuberculosis PPTases are attractive drug targets Mycobacterium tuberculosis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.8.7 gene Rv2794c or pptT, recombinant expression of MBP-tagged type II PPTase PptT in Escherichia coli strain BL21(DE3) Mycobacterium tuberculosis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.8.7 purified recombinant MBP-tagged type-II PPTase PptT, hanging drop vapor diffusion, mixing of 0.002 ml of 10 mg/ml protein in 20 mM MES, pH 6.7, 300 mM NaCl, 10% v/v glycerol, 0.5 mM tris(2-carboxyethyl)phosphine, and 1 mM CoA, with 0.001 ml of reservoir solution containing 1.6 M sodium citrate, 18°C, method optimization, X-ray diffraction structure determination and analysis at 1.75 A resolution, modeling. No crystals can be grown without added CoA. Recombinantly expressed enzyme PptT as N- or C-terminally His6-tagged proteins are soluble protein in Escherichia coli, but both are unstable over time and neither can be crystallized Mycobacterium tuberculosis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.8.7 Mg2+ dependent on, binding structure, overview. The edge strands beta4 and beta6 of the two beta-sheets provide the binding site for the CoA diphosphate and associated Mg2+ ion. The active site in Mtb-PptT is formed in the shallow cleft between the two domains, where CoA and Mg2+ are bound Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] Mycobacterium tuberculosis
-
 adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] Mycobacterium tuberculosis ATCC 25618
-
 adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.8.7 Mycobacterium tuberculosis O33336
-
-
2.7.8.7 Mycobacterium tuberculosis ATCC 25618 O33336
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.8.7 recombinant MBP-tagged type II PPTase PptT from Escherichia coli strain BL21(DE3) amylose affinity chromatography, anion exchange chromatography, and gel filtration Mycobacterium tuberculosis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
-
 Mycobacterium tuberculosis adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] The edge strands beta4 and beta6 of the two beta-sheets provide the binding site for the CoA diphosphate and associated Mg2+ ion. The active site in Mtb-PptT is formed in the shallow cleft between the two domains, where CoA and Mg2+ are bound Mycobacterium tuberculosis adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
-
 Mycobacterium tuberculosis ATCC 25618 adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] The edge strands beta4 and beta6 of the two beta-sheets provide the binding site for the CoA diphosphate and associated Mg2+ ion. The active site in Mtb-PptT is formed in the shallow cleft between the two domains, where CoA and Mg2+ are bound Mycobacterium tuberculosis ATCC 25618 adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.8.7 More Mycobacterium tuberculosis type-II PPTase PptT reveals an alpha/beta fold broadly similar to other type-II PPTases, but with differences in peripheral structural elements. Three-dimensional structure of Mtb-PptT, modeling, overview. Mtb-PptT comprises two alpha/beta domains with pseudo 2fold symmetry Mycobacterium tuberculosis

Synonyms

EC Number Synonyms Comment Organism
2.7.8.7 phosphopantetheinyl transferase
-
 Mycobacterium tuberculosis
2.7.8.7 PptT
-
 Mycobacterium tuberculosis
2.7.8.7 PTase
-
 Mycobacterium tuberculosis
2.7.8.7 Rv2794c
-
 Mycobacterium tuberculosis
2.7.8.7 type-II PPTase PptT
-
 Mycobacterium tuberculosis

General Information

EC Number General Information Comment Organism
2.7.8.7 additional information the human pathogen Mycobacterium tuberculosis encodes two PPTases, a type-I PPTase and a type-II PPTase, that are both essential. Type-II PPTase PptT shows a bound CoA that is clearly defined with its pantetheinyl arm tucked into a hydrophobic pocket. Interactions involving the CoA diphosphate, bound Mg2+ and three active site acidic side chains suggest a plausible pathway for proton transfer during catalysis. Three-dimensional structure of Mtb-PptT, modeling, overview. Mtb-PptT comprises two alpha/beta domains with pseudo 2fold symmetry. It is octahedrally coordinated to the alpha- and beta-phosphates, Asp114, Glu116, the peptide oxygen of Ala115 and a water molecule Mycobacterium tuberculosis