This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1e3p

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
[[Image:1e3p.jpg|left|200px]]
[[Image:1e3p.jpg|left|200px]]
-
{{Structure
+
<!--
-
|PDB= 1e3p |SIZE=350|CAPTION= <scene name='initialview01'>1e3p</scene>, resolution 2.50&Aring;
+
The line below this paragraph, containing "STRUCTURE_1e3p", creates the "Structure Box" on the page.
-
|SITE= <scene name='pdbsite=WO4:Putative+Orthophosphate+Site+Of+Pnpase'>WO4</scene>
+
You may change the PDB parameter (which sets the PDB file loaded into the applet)
-
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=WO4:TUNGSTATE(VI)ION'>WO4</scene>
+
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= GPSI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1890 Streptomyces antibioticus])
+
-->
-
|DOMAIN=
+
{{STRUCTURE_1e3p| PDB=1e3p | SCENE= }}
-
|RELATEDENTRY=
+
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e3p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e3p OCA], [http://www.ebi.ac.uk/pdbsum/1e3p PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1e3p RCSB]</span>
+
-
}}
+
'''TUNGSTATE DERIVATIVE OF STREPTOMYCES ANTIBIOTICUS PNPASE/ GPSI ENZYME'''
'''TUNGSTATE DERIVATIVE OF STREPTOMYCES ANTIBIOTICUS PNPASE/ GPSI ENZYME'''
Line 28: Line 25:
[[Category: Luisi, B F.]]
[[Category: Luisi, B F.]]
[[Category: Symmons, M F.]]
[[Category: Symmons, M F.]]
-
[[Category: atp-gtp diphosphotransferase rna processing]]
+
[[Category: Atp-gtp diphosphotransferase rna processing]]
-
[[Category: polyribonucleotide transferase]]
+
[[Category: Polyribonucleotide transferase]]
-
[[Category: rna degradation]]
+
[[Category: Rna degradation]]
-
 
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:37:22 2008''
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:54:25 2008''
+

Revision as of 11:37, 2 May 2008

Template:STRUCTURE 1e3p

TUNGSTATE DERIVATIVE OF STREPTOMYCES ANTIBIOTICUS PNPASE/ GPSI ENZYME


Overview

BACKGROUND: Polynucleotide phosphorylase (PNPase) is a polyribonucleotide nucleotidyl transferase (E.C.2.7.7.8) that degrades mRNA in prokaryotes. Streptomyces antibioticus PNPase also assays as a guanosine 3'-diphosphate 5'-triphosphate (pppGpp) synthetase (E.C.2.7.6.5). It may function to coordinate changes in mRNA lifetimes with pppGpp levels during the Streptomyces lifecycle. RESULTS: The structure of S. antibioticus PNPase without bound RNA but with the phosphate analog tungstate bound at the PNPase catalytic sites was determined by X-ray crystallography and shows a trimeric multidomain protein with a central channel. The structural core has a novel duplicated architecture formed by association of two homologous domains. The tungstate derivative structure reveals the PNPase active site in the second of these core domains. Structure-based sequence analysis suggests that the pppGpp synthetase active site is located in the first core domain. CONCLUSIONS: This is the first structure of a PNPase and shows the structural basis for the trimer assembly, the arrangement of accessory RNA binding domains, and the likely catalytic residues of the PNPase active site. A possible function of the trimer channel is as a contribution to both the processivity of degradation and the regulation of PNPase action by RNA structural elements.

About this Structure

1E3P is a Single protein structure of sequence from Streptomyces antibioticus. Full crystallographic information is available from OCA.

Reference

A duplicated fold is the structural basis for polynucleotide phosphorylase catalytic activity, processivity, and regulation., Symmons MF, Jones GH, Luisi BF, Structure. 2000 Nov 15;8(11):1215-26. PMID:11080643 Page seeded by OCA on Fri May 2 14:37:22 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools