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
| Line 1: | Line 1: | ||
| - | [[Image:1e3p.jpg|left|200px]] | + | [[Image:1e3p.jpg|left|200px]] |
| - | + | ||
| - | '''TUNGSTATE DERIVATIVE OF STREPTOMYCES ANTIBIOTICUS PNPASE/ GPSI ENZYME''' | + | {{Structure |
| + | |PDB= 1e3p |SIZE=350|CAPTION= <scene name='initialview01'>1e3p</scene>, resolution 2.50Å | ||
| + | |SITE= <scene name='pdbsite=WO4:Putative+Orthophosphate+Site+Of+Pnpase'>WO4</scene> | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=WO4:TUNGSTATE(VI)ION'>WO4</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= GPSI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1890 Streptomyces antibioticus]) | ||
| + | }} | ||
| + | |||
| + | '''TUNGSTATE DERIVATIVE OF STREPTOMYCES ANTIBIOTICUS PNPASE/ GPSI ENZYME''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1E3P is a [ | + | 1E3P is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_antibioticus Streptomyces antibioticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E3P OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11080643 11080643] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Streptomyces antibioticus]] | [[Category: Streptomyces antibioticus]] | ||
| Line 22: | Line 31: | ||
[[Category: rna degradation]] | [[Category: rna degradation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:49:05 2008'' |
Revision as of 08:49, 20 March 2008
| |||||||
| , resolution 2.50Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | and | ||||||
| Gene: | GPSI (Streptomyces antibioticus) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Thu Mar 20 10:49:05 2008
