1f5a: Difference between revisions
No edit summary |
No edit summary |
||
Line 1: | Line 1: | ||
[[Image:1f5a.jpg|left|200px]] | [[Image:1f5a.jpg|left|200px]] | ||
<!-- | |||
The line below this paragraph, containing "STRUCTURE_1f5a", creates the "Structure Box" on the page. | |||
You may change the PDB parameter (which sets the PDB file loaded into the applet) | |||
or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |||
or leave the SCENE parameter empty for the default display. | |||
| | --> | ||
| | {{STRUCTURE_1f5a| PDB=1f5a | SCENE= }} | ||
}} | |||
'''CRYSTAL STRUCTURE OF MAMMALIAN POLY(A) POLYMERASE''' | '''CRYSTAL STRUCTURE OF MAMMALIAN POLY(A) POLYMERASE''' | ||
Line 29: | Line 26: | ||
[[Category: Keller, W.]] | [[Category: Keller, W.]] | ||
[[Category: Martin, G.]] | [[Category: Martin, G.]] | ||
[[Category: | [[Category: Alternative splicing helical turn motif]] | ||
[[Category: | [[Category: Mrna processing]] | ||
[[Category: | [[Category: Nuclear protein]] | ||
[[Category: | [[Category: Nucleotidyl transferase catalytic domain]] | ||
[[Category: | [[Category: Phosphorylation]] | ||
[[Category: | [[Category: Rna-binding]] | ||
[[Category: | [[Category: Transcription]] | ||
[[Category: | [[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 |
Revision as of 15:55, 2 May 2008
CRYSTAL STRUCTURE OF MAMMALIAN POLY(A) POLYMERASE
OverviewOverview
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.
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 Fri May 2 15:55:10 2008