peptidase Do / protein quality control for misfolded or incompletely synthesized proteins / proteolysis involved in protein catabolic process / peptidase activity / periplasmic space / serine-type endopeptidase activity / identical protein binding Similarity search - Function
AS PER THE AUTHORS THE PROTEIN IS ONLY PRESENT AS A TRIMER IN SOLUTION IN THE ABSENCE OF SUBSTRATES
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Components
#1: Protein
ProteasedegQ
Mass: 36007.609 Da / Num. of mol.: 12 / Fragment: UNP residues 28-364 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Strain: K12 / Gene: degQ, hhoA, b3234, JW3203 / Production host: Escherichia coli (E. coli) References: UniProt: P39099, Hydrolases; Acting on peptide bonds (peptidases); Serine endopeptidases
#2: Protein/peptide
peptide (UNK)
Mass: 613.749 Da / Num. of mol.: 13 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli)
Compound details
THE PRESENCE OF THE UNKNOWN PEPTIDE CANNOT BE DISPUTED. THESE CHAINS HAVE WEAK ELECTRON DENSITY AND ...THE PRESENCE OF THE UNKNOWN PEPTIDE CANNOT BE DISPUTED. THESE CHAINS HAVE WEAK ELECTRON DENSITY AND HIGH B-FACTORS. THEIR PRESENCE BECAME EVIDENT FROM INSPECTION OF DIFFERENCE ELECTRON DENSITY MAPS AND FITS WELL TO SIMILAR OBSERVATIONS IN HOMOLOGOUS STRUCTURES. THEIR POOR DEFINITION MAY REFLECT THE FACT THAT THESE PEPTIDE WERE NOT ADDED AT ANY STEP OF THE PROTEIN PREPARATION OR CRYSTALLIZATION TRIALS, HENCE THEY MUST HAVE BEEN PICKED UP FROM THE EXPRESSION SYSTEM OR BE A CONSEQUENCE OF SOME FORM OF PROTEOLYSIS. THEREFORE THEIR OCCUPANCY IS PROBABLY LOW
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Experimental details
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Experiment
Experiment
Method: X-RAY DIFFRACTION / Number of used crystals: 1
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Sample preparation
Crystal
Density Matthews: 2.51 Å3/Da / Density % sol: 50.94 %
Crystal grow
Temperature: 291 K / Method: vapor diffusion / pH: 5.4 Details: 24% PEG6000, 5% PEG100, 10% glycerol, 0.1M MES pH5.4, VAPOR DIFFUSION, temperature 291K
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