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1e3h
From Proteopedia
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|PDB= 1e3h |SIZE=350|CAPTION= <scene name='initialview01'>1e3h</scene>, resolution 2.60Å | |PDB= 1e3h |SIZE=350|CAPTION= <scene name='initialview01'>1e3h</scene>, resolution 2.60Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e3h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e3h OCA], [http://www.ebi.ac.uk/pdbsum/1e3h PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1e3h RCSB]</span> | ||
}} | }} | ||
| Line 25: | Line 28: | ||
[[Category: Luisi, B F.]] | [[Category: Luisi, B F.]] | ||
[[Category: Symmons, M F.]] | [[Category: Symmons, M F.]] | ||
| - | [[Category: SO4]] | ||
[[Category: atp:gtp diphosphotransferase]] | [[Category: atp:gtp diphosphotransferase]] | ||
[[Category: polyribonucleotide transferase]] | [[Category: polyribonucleotide transferase]] | ||
| Line 31: | Line 33: | ||
[[Category: rna processing]] | [[Category: rna processing]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:54:17 2008'' |
Revision as of 16:54, 30 March 2008
| |||||||
| , resolution 2.60Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | GPSI (Streptomyces antibioticus) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
SEMET 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
1E3H 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 Sun Mar 30 19:54:17 2008
