1f5a: Difference between revisions

Revision as of 02:43, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1f5a.png

Template:STRUCTURE 1f5a

CRYSTAL STRUCTURE OF MAMMALIAN POLY(A) POLYMERASECRYSTAL STRUCTURE OF MAMMALIAN POLY(A) POLYMERASE

Template:ABSTRACT PUBMED 10944102

About this StructureAbout this Structure

1F5A is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of mammalian poly(A) polymerase in complex with an analog of ATP., Martin G, Keller W, Doublie S, EMBO J. 2000 Aug 15;19(16):4193-203. PMID:10944102

Page seeded by OCA on Tue Jul 1 02:43:10 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1f5a.jpg|left|200px]]
+{{Seed}}
+[[Image:1f5a.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1f5a|  PDB=1f5a  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF MAMMALIAN POLY(A) POLYMERASE'''
+===CRYSTAL STRUCTURE OF MAMMALIAN POLY(A) POLYMERASE===
-==Overview==
+<!--
-In eukaryotes, polyadenylation of pre-mRNA plays an essential role in the initiation step of protein synthesis, as well as in the export and stability of mRNAs. Poly(A) polymerase, the enzyme at the heart of the polyadenylation machinery, is a template-independent RNA polymerase which specifically incorporates ATP at the 3' end of mRNA. We have solved the crystal structure of bovine poly(A) polymerase bound to an ATP analog at 2.5 A resolution. The structure revealed expected and unexpected similarities to other proteins. As expected, the catalytic domain of poly(A) polymerase shares substantial structural homology with other nucleotidyl transferases such as DNA polymerase beta and kanamycin transferase. The C-terminal domain unexpectedly folds into a compact domain reminiscent of the RNA-recognition motif fold. The three invariant aspartates of the catalytic triad ligate two of the three active site metals. One of these metals also contacts the adenine ring. Furthermore, conserved, catalytically important residues contact the nucleotide. These contacts, taken together with metal coordination of the adenine base, provide a structural basis for ATP selection by poly(A) polymerase.
+The line below this paragraph, {{ABSTRACT_PUBMED_10944102}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10944102 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10944102}}
 ==About this Structure==
@@ Line 34: / Line 38: @@
 [[Category: Transcription]]
 [[Category: Transferase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 15:55:10 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 02:43:10 2008''