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Literature summary for 2.4.1.345 extracted from

  • Guerin, M.E.; Schaeffer, F.; Chaffotte, A.; Gest, P.; Giganti, D.; Kordulakova, J.; van der Woerd, M.; Jackson, M.; Alzari, P.M.
    Substrate-induced conformational changes in the essential peripheral membrane-associated mannosyltransferase PimA from mycobacteria: implications for catalysis (2009), J. Biol. Chem., 284, 21613-21625.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
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Mycolicibacterium smegmatis

Crystallization (Commentary)

Crystallization (Comment) Organism
PimA undergoes significant conformational changes upon substrate binding. The binding of the donor GDP-Man triggers an important interdomain rearrangement that stabilizes the enzyme and generates the binding site for the acceptor substrate, phosphatidyl-myo-inositol. The interaction of PimA with the beta-phosphate of GDP-Man is essential for this conformational change. Binding of phosphatidyl-myo-inositol has the opposite effect, inducing the formation of a more relaxed complex with PimA. GDP-Man stabilizes and phosphatidyl-myo-inositol destabilizes PimA by a similar enthalpic amount Mycolicibacterium smegmatis

Protein Variants

Protein Variants Comment Organism
E199A complete loss of activity Mycolicibacterium smegmatis
K123A 23% loss of activity Mycolicibacterium smegmatis
N63A complete loss of activity Mycolicibacterium smegmatis
N79A 29% loss of actiity Mycolicibacterium smegmatis
Q18A 90% loss of activity Mycolicibacterium smegmatis
R196A complete loss of activity Mycolicibacterium smegmatis
R68A complete loss of activity Mycolicibacterium smegmatis
R70A no loss of activity Mycolicibacterium smegmatis
S65A no loss of activity Mycolicibacterium smegmatis
T119A no loss of activity Mycolicibacterium smegmatis
Y62A complete loss of activity Mycolicibacterium smegmatis

General Stability

General Stability Organism
GDP-Man stabilizes PimA, phosphatidyl-myo-inositol destabilizes PimA after formation of a more relaxed complex Mycolicibacterium smegmatis

Organism

Organism UniProt Comment Textmining
Mycolicibacterium smegmatis A0QWG6
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-
Mycolicibacterium smegmatis ATCC 700084 A0QWG6
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-

Purification (Commentary)

Purification (Comment) Organism
combination of metal ion affinity and anionic exchange and gel filtration chromatography Mycolicibacterium smegmatis

Subunits

Subunits Comment Organism
monomer
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Mycolicibacterium smegmatis

Synonyms

Synonyms Comment Organism
membrane-associated mannosyltransferase PimA
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Mycolicibacterium smegmatis
phosphatidyl-myo-inositol mannosyltransferase A
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Mycolicibacterium smegmatis
PimA
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Mycolicibacterium smegmatis
Rv2610c
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Mycolicibacterium smegmatis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Mycolicibacterium smegmatis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Mycolicibacterium smegmatis