1e3p

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|PDB= 1e3p |SIZE=350|CAPTION= <scene name='initialview01'>1e3p</scene>, resolution 2.50&Aring;
|PDB= 1e3p |SIZE=350|CAPTION= <scene name='initialview01'>1e3p</scene>, resolution 2.50&Aring;
|SITE= <scene name='pdbsite=WO4:Putative+Orthophosphate+Site+Of+Pnpase'>WO4</scene>
|SITE= <scene name='pdbsite=WO4:Putative+Orthophosphate+Site+Of+Pnpase'>WO4</scene>
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=WO4:TUNGSTATE(VI)ION'>WO4</scene>
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=WO4:TUNGSTATE(VI)ION'>WO4</scene>
|ACTIVITY=
|ACTIVITY=
|GENE= GPSI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1890 Streptomyces antibioticus])
|GENE= GPSI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1890 Streptomyces antibioticus])
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|DOMAIN=
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|RELATEDENTRY=
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|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>
}}
}}
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[[Category: Luisi, B F.]]
[[Category: Luisi, B F.]]
[[Category: Symmons, M F.]]
[[Category: Symmons, M F.]]
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[[Category: SO4]]
 
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[[Category: WO4]]
 
[[Category: atp-gtp diphosphotransferase rna processing]]
[[Category: atp-gtp diphosphotransferase rna processing]]
[[Category: polyribonucleotide transferase]]
[[Category: polyribonucleotide transferase]]
[[Category: rna degradation]]
[[Category: rna degradation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:49:05 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:54:25 2008''

Revision as of 16:54, 30 March 2008


PDB ID 1e3p

Drag the structure with the mouse to rotate
, resolution 2.50Å
Sites:
Ligands: ,
Gene: GPSI (Streptomyces antibioticus)
Resources: FirstGlance, OCA, PDBsum, RCSB
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

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