This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2a9l

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2a9l.gif|left|200px]]<br /><applet load="2a9l" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:2a9l.gif|left|200px]]
-
caption="2a9l" />
+
 
-
'''SOLUTION NMR STRUCTURE OF A SUBSTRATE FOR THE ARCHAEAL PRE-TRNA SPLICING ENDONUCLEASES: THE BULGE-HELIX-BULGE MOTIF, MINIMIZED AVERAGE STRUCTURE'''<br />
+
{{Structure
 +
|PDB= 2a9l |SIZE=350|CAPTION= <scene name='initialview01'>2a9l</scene>
 +
|SITE= <scene name='pdbsite=NUL:Enzymatic+Cleavage+Occurs+3'+To+These+Residues'>NUL</scene>
 +
|LIGAND=
 +
|ACTIVITY=
 +
|GENE=
 +
}}
 +
 
 +
'''SOLUTION NMR STRUCTURE OF A SUBSTRATE FOR THE ARCHAEAL PRE-TRNA SPLICING ENDONUCLEASES: THE BULGE-HELIX-BULGE MOTIF, MINIMIZED AVERAGE STRUCTURE'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
2A9L is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Known structural/functional Site: <scene name='pdbsite=NUL:Enzymatic+Cleavage+Occurs+3'+To+These+Residues'>NUL</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A9L OCA].
+
2A9L is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A9L OCA].
==Reference==
==Reference==
-
Solution structure of a substrate for the archaeal pre-tRNA splicing endonucleases: the bulge-helix-bulge motif., Diener JL, Moore PB, Mol Cell. 1998 May;1(6):883-94. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9660971 9660971]
+
Solution structure of a substrate for the archaeal pre-tRNA splicing endonucleases: the bulge-helix-bulge motif., Diener JL, Moore PB, Mol Cell. 1998 May;1(6):883-94. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9660971 9660971]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Diener, J L.]]
[[Category: Diener, J L.]]
Line 21: Line 30:
[[Category: rna structure]]
[[Category: rna structure]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:25:13 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:47:03 2008''

Revision as of 13:47, 20 March 2008


PDB ID 2a9l

Drag the structure with the mouse to rotate
Sites:
Coordinates: save as pdb, mmCIF, xml



SOLUTION NMR STRUCTURE OF A SUBSTRATE FOR THE ARCHAEAL PRE-TRNA SPLICING ENDONUCLEASES: THE BULGE-HELIX-BULGE MOTIF, MINIMIZED AVERAGE STRUCTURE


Overview

The structure of the bulge-helix-bulge motif that constitutes the intron/exon splice site in H. volcanii pre-tRNATrp has been determined by NMR spectroscopy. The conformations of the two 3 nt bulges, where the pre-tRNA is cleaved, are stabilized by stacking interactions between bulge nucleotides and bases in the adjacent Watson-Crick helices and by a network of backbone hydrogen bonds. Both bulges are presented on the same minor groove face of the central 4 bp helix, and the overall structure has approximate two-fold symmetry, which makes it well-suited for attack by archaeal splicing endonucleases, which are symmetric dimers.

About this Structure

2A9L is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.

Reference

Solution structure of a substrate for the archaeal pre-tRNA splicing endonucleases: the bulge-helix-bulge motif., Diener JL, Moore PB, Mol Cell. 1998 May;1(6):883-94. PMID:9660971

Page seeded by OCA on Thu Mar 20 15:47:03 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools