1ou5

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
[[Image:1ou5.jpg|left|200px]]
[[Image:1ou5.jpg|left|200px]]
-
{{Structure
+
<!--
-
|PDB= 1ou5 |SIZE=350|CAPTION= <scene name='initialview01'>1ou5</scene>, resolution 3.40&Aring;
+
The line below this paragraph, containing "STRUCTURE_1ou5", creates the "Structure Box" on the page.
-
|SITE=
+
You may change the PDB parameter (which sets the PDB file loaded into the applet)
-
|LIGAND=
+
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-
|ACTIVITY=
+
or leave the SCENE parameter empty for the default display.
-
|GENE= hMtCCA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
+
-->
-
|DOMAIN=
+
{{STRUCTURE_1ou5| PDB=1ou5 | SCENE= }}
-
|RELATEDENTRY=[[1miv|1MIV]], [[1miw|1MIW]], [[1miy|1MIY]]
+
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ou5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ou5 OCA], [http://www.ebi.ac.uk/pdbsum/1ou5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ou5 RCSB]</span>
+
-
}}
+
'''Crystal structure of human CCA-adding enzyme'''
'''Crystal structure of human CCA-adding enzyme'''
Line 31: Line 28:
[[Category: Reichert, A S.]]
[[Category: Reichert, A S.]]
[[Category: Steegborn, C.]]
[[Category: Steegborn, C.]]
-
[[Category: nucleotidyltransferase]]
+
[[Category: Nucleotidyltransferase]]
-
[[Category: polymerase]]
+
[[Category: Polymerase]]
-
[[Category: trna]]
+
[[Category: Trna]]
-
 
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:17:04 2008''
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:50:21 2008''
+

Revision as of 01:17, 3 May 2008

Template:STRUCTURE 1ou5

Crystal structure of human CCA-adding enzyme


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.

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 Sat May 3 04:17:04 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools