1ou5

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /> <applet load="1ou5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ou5, resolution 3.40&Aring;" /> '''Crystal structure o...)
Line 1: Line 1:
-
[[Image:1ou5.gif|left|200px]]<br />
+
[[Image:1ou5.jpg|left|200px]]<br /><applet load="1ou5" size="350" color="white" frame="true" align="right" spinBox="true"
-
<applet load="1ou5" size="450" color="white" frame="true" align="right" spinBox="true"
+
caption="1ou5, resolution 3.40&Aring;" />
caption="1ou5, resolution 3.40&Aring;" />
'''Crystal structure of human CCA-adding enzyme'''<br />
'''Crystal structure of human CCA-adding enzyme'''<br />
Line 11: Line 10:
==About this Structure==
==About this Structure==
-
1OU5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OU5 OCA].
+
1OU5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OU5 OCA].
==Reference==
==Reference==
Line 27: Line 26:
[[Category: trna]]
[[Category: trna]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:36:26 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:35:40 2008''

Revision as of 14:35, 15 February 2008


1ou5, resolution 3.40Å

Drag the structure with the mouse to rotate

Crystal structure of human CCA-adding enzyme

Contents

Overview

All tRNA molecules carry the invariant sequence CCA at their 3'-terminus, for amino acid attachment. The post-transcriptional addition of CCA is, carried out by ATP(CTP):tRNA nucleotidyltransferase, also called CCase., This enzyme catalyses a unique template-independent but sequence-specific, nucleotide polymerization reaction. In order to reveal the molecular, mechanism of this activity, we solved the crystal structure of human CCase, by single isomorphous replacement. The structure reveals a four domain, architecture with a cluster of conserved residues forming a positively, charged cleft between the first two domains. Structural homology of the, N-terminal CCase domain to other nucleotidyltransferases could be, exploited for modeling a tRNA-substrate complex. The model places the tRNA, 3'-end into the N-terminal nucleotidyltransferase site, close to a patch, of conserved residues that provide the binding sites for CTP and ATP., Based on our results, we introduce a corkscrew model for CCA addition that, includes a fixed active site and a traveling tRNA-binding region formed by, flexible parts of the protein.

Disease

Known disease associated with this structure: Deafness, mitochondrial, modifier of OMIM:[610230]

About this Structure

1OU5 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of the human CCA-adding enzyme: insights into template-independent polymerization., Augustin MA, Reichert AS, Betat H, Huber R, Morl M, Steegborn C, J Mol Biol. 2003 May 16;328(5):985-94. PMID:12729736

Page seeded by OCA on Fri Feb 15 16:35:40 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools