NMR structure of E. coli Trigger Factor in complex with unfolded PhoA220-310

E. coli Trigger Factor in complex with unfolded PhoA220-310

Structural basis for protein antiaggregation activity of the trigger factor chaperone.

1000 was added to the actual sequence number: 1220 (in PDB) = 220 (in public databases)

Three-Dimensional Structure Of The D153g Mutant Of E. Coli Alkaline Phosphatase: A Mutant With Weaker Magnesium Binding And Inc

Kinetics And Crystal Structure Of A Mutant E. Coli Alkaline Phosphatase (Asp-369-->asn): A Mechanism Involving One Zinc Per Act

Reaction Mechanism Of Alkaline Phosphatase Based On Crystal Structures. Two Metal Ion Catalysis

Alkaline Phosphatase Complexed With Vanadate

Structure Of E. Coli Alkaline Phosphatase Inhibited By The Inorganic Phosphate At 1.75a Resolution

Structure Of E. Coli Alkaline Phosphatase Without The Inorganic Phosphate At 1.75a Resolution

E. Coli Alkaline Phosphatase Mutant (S102a)

E. Coli Alkaline Phosphatase Mutant (S102c)

E. Coli Alkaline Phosphatase Mutant (S102g)

Alkaline Phosphatase (e.c. 3.1.3.1) Complex With Phosphonoacetic Acid

Alkaline Phosphatase (E.C. 3.1.3.1) Complex With Mercaptomethyl Phosphonate

E. Coli Alkaline Phosphatase Mutant (d330n) In Complex With Phosphate

E. Coli Alkaline Phosphatase Mutant (d330n) Mimic Of The Transition States With Aluminium Fluoride

E. Coli Alkaline Phosphatase Mutant (d153gd330n)

E. Coli Alkaline Phosphatase Mutant (d153gd330n) Complex With Phosphate

E. Coli Alkaline Phosphatase Mutant (d153hd330n) Mimic Of The Transition States With Aluminium Fluoride

E. Coli Alkaline Phosphatase Mutant (d153hd330n)

E. Coli Alkaline Phosphatase Mutant (d153hd330n) Complex With Phosphate

E. Coli Alkaline Phosphatase Mutant (d153hd330n) Zinc Form

Structure Of E. Coli Alkaline Phosphatase In Presence Of Cobalt At 1.60 A Resolution

Structure Of D153hK328W E. COLI ALKALINE PHOSPHATASE IN Presence Of Cobalt At 1.77 A Resolution

Structure Of S102t E. Coli Alkaline Phosphatase In Presence Of Phosphate At 2.00 A Resolution

Structure Of S102t E. Coli Alkaline Phosphatase-Phosphate Intermediate At 2.20a Resolution

Crystal Structure Of Metal-Free E. Coli Alkaline Phosphatase (T155v)

Crystal Structure Of Wild-TypeT155V MIXED DIMER OF E. COLI ALKALINE Phosphatase

Crystal Structure Of Zinc-Deficient Wild-Type E. Coli Alkaline Phosphatase

E. Coli Alkaline Phosphatase Mutant R166s In Complex With Phosphate

Structure Of E.coli Alkaline Phosphatase Mutant In Complex With A Phosphorylated Peptide

Structure Of E322y Alkaline Phosphatase In Complex With Inorganic Phosphate

E. Coli Alkaline Phosphatase With Bound Inorganic Phosphate

E. Coli Alkaline Phosphatase Mutant S102g/r166s In Complex With Inorganic Phosphate

Crystal Structure Of E. Coli Alkaline Phosphatase D101a/d153a In Complex With Inorganic Phosphate

alkaline phosphatase [Escherichia coli O157:H7 str. Sakai]

alkaline phosphatase [Escherichia coli str. K12 substr. W3110]

alkaline phosphatase [Escherichia coli SE11]

bacterial alkaline phosphatase PhoA [Escherichia coli O26:H11 str. 11368]

bacterial alkaline phosphatase PhoA [Escherichia coli O103:H2 str. 12009]

alkaline phosphatase [Escherichia coli LF82]

alkaline phosphatase [Escherichia coli BL21(DE3)]

bacterial alkaline phosphatase [Escherichia coli IAI1]

bacterial alkaline phosphatase [Escherichia coli S88]

alkaline phosphatase precursor (EC 3.1.3.1) [Escherichia coli]

bacterial alkaline phosphatase [Escherichia coli str. K-12 substr. MG1655]

alkaline phosphatase [Shigella flexneri 2a str. 301]

alkaline phosphatase [Shigella flexneri]

RecName: Full=Alkaline phosphatase; Short=APase; Flags: Precursor

Trigger Factor In Complex With The Ribosome Forms A Molecular Cradle For Nascent Proteins

Nmr Structure Of E. Coli Trigger Factor In Complex With Unfolded Phoa1-150

Nmr Structure Of E. Coli Trigger Factor In Complex With Unfolded Phoa365-471

Structure Of The E. Coli Trigger Factor Bound To A Translating Ribosome

trigger factor [Escherichia coli O157:H7 str. Sakai]

trigger factor tag [Expression vector pColdTF]

peptidyl-prolyl cis/trans isomerase [Escherichia coli str. K-12 substr. W3110]

peptidyl-prolyl cis/trans isomerase [Escherichia coli O26:H11 str. 11368]

trigger factor; a molecular chaperone involved in cell division [Escherichia coli BL21(DE3)]

peptidyl-prolyl cis/trans isomerase (trigger factor) [Escherichia coli IAI1]

peptidyl-prolyl cis/trans isomerase (trigger factor) [Escherichia coli S88]

peptidyl-prolyl cis/trans isomerase (trigger factor) [Escherichia coli ED1a]

peptidyl-prolyl cis/trans isomerase (trigger factor) [Escherichia coli str. K-12 substr. MG1655]

trigger factor; a molecular chaperone involved in cell division [Escherichia coli O157:H7 str. EDL933]

trigger factor [Shigella flexneri 2a str. 301]

trigger factor [Escherichia coli O157:H7 str. EDL933]

trigger factor [Escherichia coli CFT073]

RecName: Full=Trigger factor; Short=TF; AltName: Full=PPIase [Escherichia coli APEC O1]

RecName: Full=Trigger factor; Short=TF; AltName: Full=PPIase [Escherichia coli E24377A]

RecName: Full=Trigger factor; Short=TF; AltName: Full=PPIase [Escherichia coli HS]

RecName: Full=Trigger factor; Short=TF; AltName: Full=PPIase [Escherichia coli ATCC 8739]

RecName: Full=Trigger factor; Short=TF; AltName: Full=PPIase [Escherichia coli SMS-3-5]

E. coli Trigger Factor in complex with unfolded PhoA1-150
E. coli Trigger Factor in complex with unfolded PhoA365-471
Schwieters, Kuszewski, Tjandra and Clore
Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax
Brunger, Adams, Clore, Gros, Nilges and Read