1e3p
From Proteopedia
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| - | [[Image:1e3p.jpg|left|200px]] | + | [[Image:1e3p.jpg|left|200px]] |
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| - | '''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== | ||
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==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]] | ||
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[[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
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| , resolution 2.50Å | |||||||
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| 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
