We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

2dra

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2dra.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2dra.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2dra| PDB=2dra | SCENE= }}
{{STRUCTURE_2dra| PDB=2dra | SCENE= }}
-
'''Complex structure of CCA-adding enzyme with tRNAminiDCC and ATP'''
+
===Complex structure of CCA-adding enzyme with tRNAminiDCC and ATP===
-
==Overview==
+
<!--
-
CCA-adding polymerase matures the essential 3'-CCA terminus of transfer RNA without any nucleic-acid template. However, it remains unclear how the correct nucleotide triphosphate is selected in each reaction step and how the polymerization is driven by the protein and RNA dynamics. Here we present complete sequential snapshots of six complex structures of CCA-adding enzyme and four distinct RNA substrates with and without CTP (cytosine triphosphate) or ATP (adenosine triphosphate). The CCA-lacking RNA stem extends by one base pair to force the discriminator nucleoside into the active-site pocket, and then tracks back after incorporation of the first cytosine monophosphate (CMP). Accommodation of the second CTP clamps the catalytic cleft, inducing a reorientation of the turn, which flips C74 to allow CMP to be accepted. In contrast, after the second CMP is added, the polymerase and RNA primer are locked in the closed state, which directs the subsequent A addition. Between the CTP- and ATP-binding stages, the side-chain conformation of Arg 224 changes markedly; this is controlled by the global motion of the enzyme and position of the primer terminus, and is likely to achieve the CTP/ATP discrimination, depending on the polymerization stage. Throughout the CCA-adding reaction, the enzyme tail domain firmly anchors the TPsiC-loop of the tRNA, which ensures accurate polymerization and termination.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17051158}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17051158 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17051158}}
==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Tomita, K.]]
[[Category: Tomita, K.]]
[[Category: Protein-rna complex]]
[[Category: Protein-rna complex]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 01:00:14 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 18:23:35 2008''

Revision as of 15:23, 27 July 2008

Image:2dra.png

Template:STRUCTURE 2dra

Complex structure of CCA-adding enzyme with tRNAminiDCC and ATP

Template:ABSTRACT PUBMED 17051158

About this Structure

2DRA is a Single protein structure of sequence from Archaeoglobus fulgidus. Full crystallographic information is available from OCA.

Reference

Complete crystallographic analysis of the dynamics of CCA sequence addition., Tomita K, Ishitani R, Fukai S, Nureki O, Nature. 2006 Oct 26;443(7114):956-60. Epub 2006 Oct 15. PMID:17051158

Page seeded by OCA on Sun Jul 27 18:23:35 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2dra"
Personal tools