PDBsum entry 1tyc

Aminoacyl-tRNA synthase

PDB id: 1tyc

Contents

Protein chain

317 a.a.

Waters ×171

References listed in PDB file

Key reference

Title

Structural analysis of a series of mutants of tyrosyl-Trna synthetase: enhancement of catalysis by hydrophobic interactions

Authors

K.A.Brown, P.De meester, A.R.Fersht ii, D.M.Blow.

Ref.

To be Published ...

Secondary reference #1

Title

Structure of tyrosyl-Trna synthetase refined at 2.3 a resolution. Interaction of the enzyme with the tyrosyl adenylate intermediate.

Authors

P.Brick, T.N.Bhat, D.M.Blow.

Ref.

J Mol Biol, 1989, 208, 83-98.

PubMed id

2504923

Secondary reference #2

Title

Crystal structure of a deletion mutant of a tyrosyl-Trna synthetase complexed with tyrosine.

Authors

P.Brick, D.M.Blow.

Ref.

J Mol Biol, 1987, 194, 287-297.

PubMed id

3612807

Secondary reference #3

Title

Structure of a mutant of tyrosyl-Trna synthetase with enhanced catalytic properties.

Authors

K.A.Brown, P.Brick, D.M.Blow.

Ref.

Nature, 1987, 326, 416-418.

PubMed id

3104791

Secondary reference #4

Title

Internal thermodynamics of position 51 mutants and natural variants of tyrosyl-Trna synthetase.

Authors

C.K.Ho, A.R.Fersht.

Ref.

Biochemistry, 1986, 25, 1891-1897. [DOI no: 10.1021/bi00356a009]

PubMed id

3518795

Secondary reference #5

Title

Natural variation of tyrosyl-Trna synthetase and comparison with engineered mutants.

Authors

M.D.Jones, D.M.Lowe, T.Borgford, A.R.Fersht.

Ref.

Biochemistry, 1986, 25, 1887-1891. [DOI no: 10.1021/bi00356a008]

PubMed id

3011073

Secondary reference #6

Title

Use of binding energy in catalysis analyzed by mutagenesis of the tyrosyl-Trna synthetase.

Authors

T.N.Wells, A.R.Fersht.

Ref.

Biochemistry, 1986, 25, 1881-1886. [DOI no: 10.1021/bi00356a007]

PubMed id

3518794

Secondary reference #7

Title

Fine structure-Activity analysis of mutations at position 51 of tyrosyl-Trna synthetase.

Authors

A.R.Fersht, A.J.Wilkinson, P.Carter, G.Winter.

Ref.

Biochemistry, 1985, 24, 5858-5861. [DOI no: 10.1021/bi00342a025]

PubMed id

3002425

Secondary reference #8

Title

The use of double mutants to detect structural changes in the active site of the tyrosyl-Trna synthetase (bacillus stearothermophilus).

Authors

P.J.Carter, G.Winter, A.J.Wilkinson, A.R.Fersht.

Ref.

Cell, 1984, 38, 835-840. [DOI no: 10.1016/0092-8674(84)90278-2]

PubMed id

6488318

Figure 1.
Figure 1. Streo Pair of art of the Active Site of TyrTS (B. stearothemophilus)

Figure 3.
igure 3. Amino Acid Side Chain A Is Mutated to A', and B to B'

The above figures are reproduced from the cited reference with permission from Cell Press

Secondary reference #9

Title

A large increase in enzyme-Substrate affinity by protein engineering.

Authors

A.J.Wilkinson, A.R.Fersht, D.M.Blow, P.Carter, G.Winter.

Ref.

Nature, 1984, 307, 187-188.

PubMed id

6690998

Secondary reference #10

Title

Interaction of crystalline tyrosyl-Trna synthetase with adenosine, Adenosine monophosphate, Adenosine triphosphate and pyrophosphate in the presence of tyrosinol.

Authors

C.Monteilhet, D.M.Blow, P.Brick.

Ref.

J Mol Biol, 1984, 173, 477-485. [DOI no: 10.1016/0022-2836(84)90392-9]

PubMed id

6323720

Figure 2.
FIG 2. Electron-density difference maps showing: (a) the binding of L-tyrosinr. (TyrRS + tyrosine) -TyrRS (Monteilh& & Blow. 1978); and (b) the binding of r.-tyrosinol: (TyrRS + tyrosinol + adenosine + PP,)-TyrRS. The ifference maps (TyrRS + tyrosinol + AMP + PP,)-yrRS and (TyrRS + tyrosinol + ATP) -T,wRS are similar to (b). The frames are composite of' 10 sections coveing an area of 18 XX 15 A in the active region wit a depth of 8d. The cq-stallographic Z direction is vertical. Contours are at diference density levels of lC50. 19(K). 2300 .(arbitrary units). and the roken lines represent negative contours.

Figure 3.
FG. 3. Electron-densit,y differnce maps shtwiny modifirations around the tyrosne biing site. (a) (TyrRS + tyrosinol + adenosinc + PP,)-(TyrKS + tyrosine): (b) (TyrRS + tyrosinol + AMP + PP,)-(TyrRS + tyrosine): (c) (TyrS + t.yrosinol + ATP)-(TyrRS + tyrosine); (d) (TyrRS + tywsirryl denylate) - (TyrRS + twosine): (Mont,ilhvt & I~low. 1078). Each frame is a composite of IO sections covering the same area as'in Fig. 2: wntjour levels are 1700. 2000, 2300. fo (a). (b) and (c): fol (cl) tltry arc 3800. 4700. 5600. using the same arbitra.r> units as in Pig 2.

The above figures are reproduced from the cited reference with permission from Elsevier

Secondary reference #11

Title

Tyrosyl-Trna synthetase forms a mononucleotide-Binding fold.

Authors

T.N.Bhat, D.M.Blow, P.Brick, J.Nyborg.

Ref.

J Mol Biol, 1982, 158, 699-709.

PubMed id

7120416

Secondary reference #12

Title

A density-Modification method for the improvement of poorly resolved protein electron-Density maps

Authors

T.N.Bhat, D.M.Blow.

Ref.

Acta Crystallogr ,Sect A, 1982, 38, 21.

Secondary reference #13

Title

Binding of tyrosine, Adenosine triphosphate and analogues to crystalline tyrosyl transfer RNA synthetase.

Authors

C.Monteilhet, D.M.Blow.

Ref.

J Mol Biol, 1978, 122, 407-417. [DOI no: 10.1016/0022-2836(78)90418-7]

PubMed id

691047

Figure 1.
FIa. 1. Incorporation of [`%]tyrosine into TyrRSase crystals.

Figure 2.
FIG. 2. Incorporation f [`%]ATP into TyrRSsse crystals.

The above figures are reproduced from the cited reference with permission from Elsevier

Secondary reference #14

Title

Structure of aminoacyl t/RNA synthetases

Authors

D.M.Blow, C.Monteilhet, J.R.Rubin.

Ref.

Proc FEBS Meet, 1978, 52, 59.

Secondary reference #15

Title

The peptide chain of tyrosyl tRNA synthetase: no evidence for a super-Secondary structure of four alpha-Helices.

Authors

D.M.Blow, M.J.Irwin, J.Nyborg.

Ref.

Biochem Biophys Res Commun, 1977, 76, 728-734.

PubMed id

901445

Secondary reference #16

Title

The crystal structure of tyrosyl-Transfer RNA synthetase at 2-7 a resolution.

Authors

M.J.Irwin, J.Nyborg, B.R.Reid, D.M.Blow.

Ref.

J Mol Biol, 1976, 105, 577-586.

PubMed id

972395

Secondary reference #17

Title

Letter: crystallization and preliminary X-Ray diffraction studies on tyrosyl-Transfer RNA synthetase from bacillus stearothermophilus.

Authors

B.R.Reid, G.L.Koch, Y.Boulanger, B.S.Hartley, D.M.Blow.

Ref.

J Mol Biol, 1973, 80, 199-201.

PubMed id

4784896