Literature summary for 7.4.2.6 extracted from

Levdikov, V.M.; Blagova, E.V.; Brannigan, J.A.; Wright, L.; Vagin, A.A.; Wilkinson, A.J.
The structure of the oligopeptide-binding protein, AppA, from Bacillus subtilis in complex with a nonapeptide (2004), J. Mol. Biol., 345, 879-892.

Cloned(Commentary)

Cloned (Comment)	Organism
gene appA, expression of soluble form of AppA fused to maltose-binding protein in Escherichia coli strain B834 periplasm	Bacillus subtilis

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified soluble form of AppA in complex with a nonapeptide, hanging drop vapour diffusion method, unlabeled enzyme from 12-14% PEG 8000, 0.1-0.2 M zinc acetate, 0.1 M MES, pH 6.5, or Tris-HCl, pH 7.5, selenium-labeled enzyme from 16-18% PEG 8000, 0.1 M zinc acetate, and 0.1 M MES, pH 6.5, or Tris-HCl, pH 7.5, cryoprotection by 25% v/v glycerol, X-ray diffraction structure determination and analysis at 2.3-1.6 A resolution, selenium-based anomalous scattering and molecular replacement methods	Bacillus subtilis

Crystallization (Comment)

Organism

purified soluble form of AppA in complex with a nonapeptide, hanging drop vapour diffusion method, unlabeled enzyme from 12-14% PEG 8000, 0.1-0.2 M zinc acetate, 0.1 M MES, pH 6.5, or Tris-HCl, pH 7.5, selenium-labeled enzyme from 16-18% PEG 8000, 0.1 M zinc acetate, and 0.1 M MES, pH 6.5, or Tris-HCl, pH 7.5, cryoprotection by 25% v/v glycerol, X-ray diffraction structure determination and analysis at 2.3-1.6 A resolution, selenium-based anomalous scattering and molecular replacement methods

Bacillus subtilis

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
membrane	enzymes form membrane-spanning tunnels	Bacillus subtilis	16020	-

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	-	Bacillus subtilis

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
60000	-	x * 60000, recombinant selenium-labeled, detagged soluble AppA, SDS-PAGE	Bacillus subtilis

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + H2O + oligopeptide/out	Bacillus subtilis	the enzyme imports exogenous peptides that play roles as source of amino acids and in the signalling pathways leading to development of competence and sporulation, overview	ADP + phosphate + oligopeptide/in	-	?

Organism

Organism	UniProt	Comment	Textmining
Bacillus subtilis	-	genes dpp, appA, and oppA	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
lipoprotein	AppA has a lipid-modified, membrane-anchored extracellular protein binding domain which served as a receptor for the oligopeptide translocation system	Bacillus subtilis

Purification (Commentary)

Purification (Comment)	Organism
recombinant selenium-labeled maltose-binding fusion protein by amylose affinity chromatography, cleavage of the fusion protein by factor Xa, further purification by ion exchange chromatography and gel filtration, to homogeneity	Bacillus subtilis

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + H2O + oligopeptide/out	the enzyme imports exogenous peptides that play roles as source of amino acids and in the signalling pathways leading to development of competence and sporulation, overview	Bacillus subtilis	ADP + phosphate + oligopeptide/in	-	?
ATP + H2O + oligopeptide/out	ATP hydrolysis is coupled to peptide translocation, the enzyme has a lipid-modified, membrane-anchored extracellular protein binding domain which serve as a receptor for the system, peptide ligand pocket structure of AppA, overview	Bacillus subtilis	ADP + phosphate + oligopeptide/in	-	?

Subunits

Subunits	Comment	Organism
?	x * 60000, recombinant selenium-labeled, detagged soluble AppA, SDS-PAGE	Bacillus subtilis
More	domain organization of AppA and OppA, overview, AppA has a lipid-modified, membrane-anchored extracellular protein binding domain which served as a receptor for the oligopeptide translocation system	Bacillus subtilis

Synonyms

Synonyms	Comment	Organism
AppA	-	Bacillus subtilis
More	AppA, OppA, and Dpp belong to the ATP-binding casette family, the ABC-type ATPases	Bacillus subtilis
oligopeptide permease	-	Bacillus subtilis
oligopeptide-binding protein	-	Bacillus subtilis
OppA	-	Bacillus subtilis