1s68

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1s68" size="450" color="white" frame="true" align="right" spinBox="true" caption="1s68, resolution 1.90&Aring;" /> '''Structure and Mechan...)
Line 1: Line 1:
-
[[Image:1s68.jpg|left|200px]]<br /><applet load="1s68" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1s68.jpg|left|200px]]<br /><applet load="1s68" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1s68, resolution 1.90&Aring;" />
caption="1s68, resolution 1.90&Aring;" />
'''Structure and Mechanism of RNA Ligase'''<br />
'''Structure and Mechanism of RNA Ligase'''<br />
==Overview==
==Overview==
-
T4 RNA ligase 2 (Rnl2) exemplifies an RNA ligase family that includes the, RNA editing ligases (RELs) of Trypanosoma and Leishmania. The Rnl2/REL, enzymes are defined by essential signature residues and a unique, C-terminal domain, which we show is essential for sealing of 3'-OH and, 5'-PO4 RNA ends by Rnl2, but not for ligase adenylation or phosphodiester, bond formation at a preadenylated AppRNA end. The N-terminal segment, Rnl2(1-249) of the 334 aa Rnl2 protein comprises an autonomous, adenylyltransferase/AppRNA ligase domain. We report the 1.9 A crystal, structure of the ligase domain with AMP bound at the active site, which, reveals a shared fold, catalytic mechanism, and evolutionary history for, RNA ligases, DNA ligases, and mRNA capping enzymes.
+
T4 RNA ligase 2 (Rnl2) exemplifies an RNA ligase family that includes the RNA editing ligases (RELs) of Trypanosoma and Leishmania. The Rnl2/REL enzymes are defined by essential signature residues and a unique C-terminal domain, which we show is essential for sealing of 3'-OH and 5'-PO4 RNA ends by Rnl2, but not for ligase adenylation or phosphodiester bond formation at a preadenylated AppRNA end. The N-terminal segment Rnl2(1-249) of the 334 aa Rnl2 protein comprises an autonomous adenylyltransferase/AppRNA ligase domain. We report the 1.9 A crystal structure of the ligase domain with AMP bound at the active site, which reveals a shared fold, catalytic mechanism, and evolutionary history for RNA ligases, DNA ligases, and mRNA capping enzymes.
==About this Structure==
==About this Structure==
-
1S68 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4] with AMP as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1S68 OCA].
+
1S68 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4] with <scene name='pdbligand=AMP:'>AMP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S68 OCA].
==Reference==
==Reference==
Line 13: Line 13:
[[Category: Bacteriophage t4]]
[[Category: Bacteriophage t4]]
[[Category: Single protein]]
[[Category: Single protein]]
-
[[Category: Ho, C.K.]]
+
[[Category: Ho, C K.]]
-
[[Category: Lima, C.D.]]
+
[[Category: Lima, C D.]]
[[Category: Shuman, S.]]
[[Category: Shuman, S.]]
-
[[Category: Wang, L.K.]]
+
[[Category: Wang, L K.]]
[[Category: AMP]]
[[Category: AMP]]
[[Category: ribonucleic acid ligase]]
[[Category: ribonucleic acid ligase]]
Line 22: Line 22:
[[Category: t4]]
[[Category: t4]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:08:52 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:58:23 2008''

Revision as of 12:58, 21 February 2008

Image:1s68.jpg

1s68, resolution 1.90Å

Drag the structure with the mouse to rotate

Structure and Mechanism of RNA Ligase

Overview

T4 RNA ligase 2 (Rnl2) exemplifies an RNA ligase family that includes the RNA editing ligases (RELs) of Trypanosoma and Leishmania. The Rnl2/REL enzymes are defined by essential signature residues and a unique C-terminal domain, which we show is essential for sealing of 3'-OH and 5'-PO4 RNA ends by Rnl2, but not for ligase adenylation or phosphodiester bond formation at a preadenylated AppRNA end. The N-terminal segment Rnl2(1-249) of the 334 aa Rnl2 protein comprises an autonomous adenylyltransferase/AppRNA ligase domain. We report the 1.9 A crystal structure of the ligase domain with AMP bound at the active site, which reveals a shared fold, catalytic mechanism, and evolutionary history for RNA ligases, DNA ligases, and mRNA capping enzymes.

About this Structure

1S68 is a Single protein structure of sequence from Bacteriophage t4 with as ligand. Full crystallographic information is available from OCA.

Reference

Structure and mechanism of RNA ligase., Ho CK, Wang LK, Lima CD, Shuman S, Structure. 2004 Feb;12(2):327-39. PMID:14962393

Page seeded by OCA on Thu Feb 21 14:58:23 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1s68"
Personal tools