2V0Y

Crystal structure of apo C298S tryptophanase from E.coli

Summary for 2V0Y

• Entry DOI: 10.2210/pdb2v0y/pdb
• Related: 2C44 2V1P
• Descriptor: TRYPTOPHANASE, CHLORIDE ION, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: lyase, pyridoxal phosphate, tryptophan catabolism
• Biological source: ESCHERICHIA COLI
• Cellular location: Cytoplasm : P0A853
• Total number of polymer chains: 1
• Total formula weight: 52432.50

Authors

Kogan, A.,Gdalevsky, G.Y.,Cohen-Luria, R.,Goldgur, Y.,Parola, A.H.,Almog, O. (deposition date: 2007-05-21, release date: 2008-06-10, Last modification date: 2024-11-13)

Primary citation

Kogan, A.,Gdalevsky, G.Y.,Cohen-Luria, R.,Goldgur, Y.,Phillips, R.S.,Parola, A.H.,Almog, O.
Conformational Changes and Loose Packing Promote E. Coli Tryptophanase Cold Lability.
Bmc Struct.Biol., 9:65-, 2009

PubMed Abstract: Oligomeric enzymes can undergo a reversible loss of activity at low temperatures. One such enzyme is tryptophanase (Trpase) from Escherichia coli. Trpase is a pyridoxal phosphate (PLP)-dependent tetrameric enzyme with a Mw of 210 kD. PLP is covalently bound through an enamine bond to Lys270 at the active site. The incubation of holo E. coli Trpases at 2 degrees C for 20 h results in breaking this enamine bond and PLP release, as well as a reversible loss of activity and dissociation into dimers. This sequence of events is termed cold lability and its understanding bears relevance to protein stability and shelf life.

PubMed: 19814824
DOI: 10.1186/1472-6807-9-65

Experimental method

X-RAY DIFFRACTION (2 Å)