4UP2

Crystal structure of Escherichia coli tryptophanase purified from alkaline stressed bacterial culture.

Summary for 4UP2

Entry DOI	10.2210/pdb4up2/pdb
Related	4UP1
Descriptor	TRYPTOPHANASE, SULFATE ION, BETA-MERCAPTOETHANOL, ... (4 entities in total)
Functional Keywords	lyase, alkaline stress, protein purification
Biological source	ESCHERICHIA COLI
Total number of polymer chains	4
Total formula weight	214168.96
Authors	Rety, S.,Deschamps, P.,Leulliot, N. (deposition date: 2014-06-11, release date: 2015-06-24, Last modification date: 2024-01-10)
Primary citation	Rety, S.,Deschamps, P.,Leulliot, N. Structure of Escherichia Coli Tryptophanase Purified from an Alkaline-Stressed Bacterial Culture. Acta Crystallogr.,Sect.F, 71:1378-, 2015 Cited by PubMed Abstract: Tryptophanase is a bacterial enzyme involved in the degradation of tryptophan to indole, pyruvate and ammonia, which are compounds that are essential for bacterial survival. Tryptophanase is often overexpressed in stressed cultures. Large amounts of endogenous tryptophanase were purified from Escherichia coli BL21 strain overexpressing another recombinant protein. Tryptophanase was crystallized in space group P6522 in the apo form without pyridoxal 5'-phosphate bound in the active site. PubMed: 26527264 DOI: 10.1107/S2053230X15017549 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.78 Å)

Structure validation