2hz7: Difference between revisions

Line 4:

==Overview==

Glutaminyl-tRNA synthetase from Deinococcus radiodurans possesses a, C-terminal extension of 215 residues appending the anticodon-binding, domain. This domain constitutes a paralog of the Yqey protein present in, various organisms and part of it is present in the C-terminal end of the, GatB subunit of GatCAB, a partner of the indirect pathway of Gln-tRNA(Gln), formation. To analyze the peculiarities of the structure-function, relationship of this GlnRS related to the Yqey domain, a structure of the, protein was solved from crystals diffracting at 2.3 A and a docking model, of the synthetase complexed to tRNA(Gln) constructed. The comparison of, the modeled complex with the structure of the E. coli complex reveals that, all residues of E. coli GlnRS contacting tRNA(Gln) are conserved in D., radiodurans GlnRS, leaving the functional role of the Yqey domain, puzzling. Kinetic investigations and tRNA-binding experiments of full, length and Yqey-truncated GlnRSs reveal that the Yqey domain is involved, in tRNA(Gln) recognition. They demonstrate that Yqey plays the role of an, affinity-enhancer of GlnRS for tRNA(Gln) acting only in cis. However, the, presence of Yqey in free state in organisms lacking GlnRS, suggests that, this domain may exert additional cellular functions.

Glutaminyl-tRNA synthetase from Deinococcus radiodurans possesses a C-terminal extension of 215 residues appending the anticodon-binding domain. This domain constitutes a paralog of the Yqey protein present in various organisms and part of it is present in the C-terminal end of the GatB subunit of GatCAB, a partner of the indirect pathway of Gln-tRNA(Gln) formation. To analyze the peculiarities of the structure-function relationship of this GlnRS related to the Yqey domain, a structure of the protein was solved from crystals diffracting at 2.3 A and a docking model of the synthetase complexed to tRNA(Gln) constructed. The comparison of the modeled complex with the structure of the E. coli complex reveals that all residues of E. coli GlnRS contacting tRNA(Gln) are conserved in D. radiodurans GlnRS, leaving the functional role of the Yqey domain puzzling. Kinetic investigations and tRNA-binding experiments of full length and Yqey-truncated GlnRSs reveal that the Yqey domain is involved in tRNA(Gln) recognition. They demonstrate that Yqey plays the role of an affinity-enhancer of GlnRS for tRNA(Gln) acting only in cis. However, the presence of Yqey in free state in organisms lacking GlnRS, suggests that this domain may exert additional cellular functions.

==About this Structure==

Line 14:

[[Category: Glutamine--tRNA ligase]]

[[Category: Single protein]]

[[Category: Becker, H.D.]]

[[Category: Becker, H D.]]

[[Category: Deniziak, M.]]

[[Category: Giege, R.]]

Line 24:

[[Category: rossmann fold]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Wed Jan 23 15~~:35:07 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:47:22 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 4: / Line 4: @@
 ==Overview==
-Glutaminyl-tRNA synthetase from Deinococcus radiodurans possesses a, C-terminal extension of 215 residues appending the anticodon-binding, domain. This domain constitutes a paralog of the Yqey protein present in, various organisms and part of it is present in the C-terminal end of the, GatB subunit of GatCAB, a partner of the indirect pathway of Gln-tRNA(Gln), formation. To analyze the peculiarities of the structure-function, relationship of this GlnRS related to the Yqey domain, a structure of the, protein was solved from crystals diffracting at 2.3 A and a docking model, of the synthetase complexed to tRNA(Gln) constructed. The comparison of, the modeled complex with the structure of the E. coli complex reveals that, all residues of E. coli GlnRS contacting tRNA(Gln) are conserved in D., radiodurans GlnRS, leaving the functional role of the Yqey domain, puzzling. Kinetic investigations and tRNA-binding experiments of full, length and Yqey-truncated GlnRSs reveal that the Yqey domain is involved, in tRNA(Gln) recognition. They demonstrate that Yqey plays the role of an, affinity-enhancer of GlnRS for tRNA(Gln) acting only in cis. However, the, presence of Yqey in free state in organisms lacking GlnRS, suggests that, this domain may exert additional cellular functions.
+Glutaminyl-tRNA synthetase from Deinococcus radiodurans possesses a C-terminal extension of 215 residues appending the anticodon-binding domain. This domain constitutes a paralog of the Yqey protein present in various organisms and part of it is present in the C-terminal end of the GatB subunit of GatCAB, a partner of the indirect pathway of Gln-tRNA(Gln) formation. To analyze the peculiarities of the structure-function relationship of this GlnRS related to the Yqey domain, a structure of the protein was solved from crystals diffracting at 2.3 A and a docking model of the synthetase complexed to tRNA(Gln) constructed. The comparison of the modeled complex with the structure of the E. coli complex reveals that all residues of E. coli GlnRS contacting tRNA(Gln) are conserved in D. radiodurans GlnRS, leaving the functional role of the Yqey domain puzzling. Kinetic investigations and tRNA-binding experiments of full length and Yqey-truncated GlnRSs reveal that the Yqey domain is involved in tRNA(Gln) recognition. They demonstrate that Yqey plays the role of an affinity-enhancer of GlnRS for tRNA(Gln) acting only in cis. However, the presence of Yqey in free state in organisms lacking GlnRS, suggests that this domain may exert additional cellular functions.
 ==About this Structure==
@@ Line 14: / Line 14: @@
 [[Category: Glutamine--tRNA ligase]]
 [[Category: Single protein]]
-[[Category: Becker, H.D.]]
+[[Category: Becker, H D.]]
 [[Category: Deniziak, M.]]
 [[Category: Giege, R.]]
@@ Line 24: / Line 24: @@
 [[Category: rossmann fold]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:35:07 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:47:22 2008''