Sandbox Reserved 1561: Difference between revisions

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== Structural highlights and structure-function relationships ==

(57 amino acid deletion) Bap1 is an insoluble protein at full length and requires a deletion of a hydrophobic 57-amino acid chain, which forms the beta-prism domain within blade-six of the eight-bladed beta-propeller.

(Two-Domain arrangement) Bap1 is formed by a two-domain structure, which is made up of an eight-bladed beta-propeller with a beta-prism domain within the sixth blade by a flexible linker.

(8-bladed beta propeller) The eight-bladed beta-propeller has a four-stranded antiparallel beta-sheet making up each blade.

(Beta-Prism) The beta-prism is an insertion domain within blade six via a flexible linker.

(Ion Binding sites) Blade six and blade eight don’t appear to be ion binding sites, however all sites appear to bind calcium ions. During purification of the protein, all cations were replaced by sodium ions.

(All Binding Sites) Bap1 active site appears to be outside of the central cavity of the eight-bladed beta-propeller.

(Citrate Binding Site figure 4, not actual ligand) The citrate molecule in Bap1 binds in the carbohydrate-binding site in the beta-prism domains. Citrate is required to produce optimal crystal form due to the extensive crystal contacts in the area.

(Lysine Importance)

(No Catalytic Triad) There doesn’t seem to be a catalytic triad within 6MLT.

(Lectin = protein that binds to carbohydrates) The beta-propeller utilizes lectins, called PropLecs, which are found in the beta-propeller folds that contain carbohydrate-binding sites. Asp348 forms essential contacts with bound carbohydrates in the beta-prism lectin domain on blade-six of the eight-bladed beta-propeller.

== Energy Transformation ==

Sandbox Reserved 1561: Difference between revisions

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 == Structural highlights and structure-function relationships ==
+(57 amino acid deletion) Bap1 is an insoluble protein at full length and requires a deletion of a hydrophobic 57-amino acid chain, which forms the beta-prism domain within blade-six of the eight-bladed beta-propeller.
+(Two-Domain arrangement) Bap1 is formed by a two-domain structure, which is made up of an eight-bladed beta-propeller with a beta-prism domain within the sixth blade by a flexible linker.
+(8-bladed beta propeller) The eight-bladed beta-propeller has a four-stranded antiparallel beta-sheet making up each blade.
+(Beta-Prism) The beta-prism is an insertion domain within blade six via a flexible linker.
+(Ion Binding sites) Blade six and blade eight don’t appear to be ion binding sites, however all sites appear to bind calcium ions. During purification of the protein, all cations were replaced by sodium ions.
+(All Binding Sites) Bap1 active site appears to be outside of the central cavity of the eight-bladed beta-propeller.
+(Citrate Binding Site figure 4, not actual ligand) The citrate molecule in Bap1 binds in the carbohydrate-binding site in the beta-prism domains. Citrate is required to produce optimal crystal form due to the extensive crystal contacts in the area.
+(Lysine Importance)
+(No Catalytic Triad) There doesn’t seem to be a catalytic triad within 6MLT.
+(Lectin = protein that binds to carbohydrates) The beta-propeller utilizes lectins, called PropLecs, which are found in the beta-propeller folds that contain carbohydrate-binding sites. Asp348 forms essential contacts with bound carbohydrates in the beta-prism lectin domain on blade-six of the eight-bladed beta-propeller.
 == Energy Transformation ==