2d1p: Difference between revisions

Line 1:

[[Image:2d1p.gif|left|200px]]<br /><applet load="2d1p" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:2d1p.gif|left|200px]]<br /><applet load="2d1p" size="350" color="white" frame="true" align="right" spinBox="true"

caption="2d1p, resolution 2.15Å" />

'''crystal structure of heterohexameric TusBCD proteins, which are crucial for the tRNA modification'''<br />

==Overview==

Uridine at wobble position 34 of tRNA(Lys), tRNA(Glu), and tRNA(Gln) is, exclusively modified into 2-thiouridine (s2U), which is crucial for both, precise codon recognition and recognition by the cognate aminoacyl-tRNA, synthetases. Recent Escherichia coli genetic studies revealed that the, products of five novel genes, tusABCDE, function in the s2U modification., Here, we solved the 2.15 angstroms crystal structure of the E. coli TusBCD, complex, a sulfur transfer mediator, forming a heterohexamer composed of a, dimer of the heterotrimer. Structure-based sequence alignment suggested, two putative active site Cys residues, Cys79 (in TusC) and Cys78 (in, TusD), which are exposed on the hexameric complex. In vivo mutant analyses, revealed that only Cys78, in the TusD subunit, participates in sulfur, transfer during the s2U modification process. Since the single Cys acts as, a catalytic residue, we proposed that TusBCD mediates sulfur relay via a, putative persulfide state of the TusD subunit.

Uridine at wobble position 34 of tRNA(Lys), tRNA(Glu), and tRNA(Gln) is exclusively modified into 2-thiouridine (s2U), which is crucial for both precise codon recognition and recognition by the cognate aminoacyl-tRNA synthetases. Recent Escherichia coli genetic studies revealed that the products of five novel genes, tusABCDE, function in the s2U modification. Here, we solved the 2.15 angstroms crystal structure of the E. coli TusBCD complex, a sulfur transfer mediator, forming a heterohexamer composed of a dimer of the heterotrimer. Structure-based sequence alignment suggested two putative active site Cys residues, Cys79 (in TusC) and Cys78 (in TusD), which are exposed on the hexameric complex. In vivo mutant analyses revealed that only Cys78, in the TusD subunit, participates in sulfur transfer during the s2U modification process. Since the single Cys acts as a catalytic residue, we proposed that TusBCD mediates sulfur relay via a putative persulfide state of the TusD subunit.

==About this Structure==

2D1P is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=2D1P OCA].

2D1P is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D1P OCA].

==Reference==

Line 23:

[[Category: trna modification]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Wed Nov~~ 21 09:23:~~26 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:54:28 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-[[Image:2d1p.gif|left|200px]]<br /><applet load="2d1p" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:2d1p.gif|left|200px]]<br /><applet load="2d1p" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="2d1p, resolution 2.15&Aring;" />
 '''crystal structure of heterohexameric TusBCD proteins, which are crucial for the tRNA modification'''<br />
 ==Overview==
-Uridine at wobble position 34 of tRNA(Lys), tRNA(Glu), and tRNA(Gln) is, exclusively modified into 2-thiouridine (s2U), which is crucial for both, precise codon recognition and recognition by the cognate aminoacyl-tRNA, synthetases. Recent Escherichia coli genetic studies revealed that the, products of five novel genes, tusABCDE, function in the s2U modification., Here, we solved the 2.15 angstroms crystal structure of the E. coli TusBCD, complex, a sulfur transfer mediator, forming a heterohexamer composed of a, dimer of the heterotrimer. Structure-based sequence alignment suggested, two putative active site Cys residues, Cys79 (in TusC) and Cys78 (in, TusD), which are exposed on the hexameric complex. In vivo mutant analyses, revealed that only Cys78, in the TusD subunit, participates in sulfur, transfer during the s2U modification process. Since the single Cys acts as, a catalytic residue, we proposed that TusBCD mediates sulfur relay via a, putative persulfide state of the TusD subunit.
+Uridine at wobble position 34 of tRNA(Lys), tRNA(Glu), and tRNA(Gln) is exclusively modified into 2-thiouridine (s2U), which is crucial for both precise codon recognition and recognition by the cognate aminoacyl-tRNA synthetases. Recent Escherichia coli genetic studies revealed that the products of five novel genes, tusABCDE, function in the s2U modification. Here, we solved the 2.15 angstroms crystal structure of the E. coli TusBCD complex, a sulfur transfer mediator, forming a heterohexamer composed of a dimer of the heterotrimer. Structure-based sequence alignment suggested two putative active site Cys residues, Cys79 (in TusC) and Cys78 (in TusD), which are exposed on the hexameric complex. In vivo mutant analyses revealed that only Cys78, in the TusD subunit, participates in sulfur transfer during the s2U modification process. Since the single Cys acts as a catalytic residue, we proposed that TusBCD mediates sulfur relay via a putative persulfide state of the TusD subunit.
 ==About this Structure==
-D1P is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2D1P OCA].
+D1P is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D1P OCA].
 ==Reference==
@@ Line 23: / Line 23: @@
 [[Category: trna modification]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 09:23:26 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:54:28 2008''