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Literature summary 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)

EC Number Cloned (Comment) Organism
2.4.1.345
-
 Mycolicibacterium smegmatis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.4.1.345 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

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

General Stability

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

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.345 Mycolicibacterium smegmatis A0QWG6
-
-
2.4.1.345 Mycolicibacterium smegmatis ATCC 700084 A0QWG6
-
-

Purification (Commentary)

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

Subunits

EC Number Subunits Comment Organism
2.4.1.345 monomer
-
 Mycolicibacterium smegmatis

Synonyms

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.4.1.345 37
-
 assay at Mycolicibacterium smegmatis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.4.1.345 7.5
-
 assay at Mycolicibacterium smegmatis