1e3h

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{{STRUCTURE_1e3h| PDB=1e3h | SCENE= }}
{{STRUCTURE_1e3h| PDB=1e3h | SCENE= }}
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'''SEMET DERIVATIVE OF STREPTOMYCES ANTIBIOTICUS PNPASE/GPSI ENZYME'''
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===SEMET DERIVATIVE OF STREPTOMYCES ANTIBIOTICUS PNPASE/GPSI ENZYME===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_11080643}}
==About this Structure==
==About this Structure==
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[[Category: Rna degradation]]
[[Category: Rna degradation]]
[[Category: Rna processing]]
[[Category: Rna processing]]
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Revision as of 21:05, 30 June 2008

Image:1e3h.png

Template:STRUCTURE 1e3h

SEMET DERIVATIVE OF STREPTOMYCES ANTIBIOTICUS PNPASE/GPSI ENZYME

Template:ABSTRACT PUBMED 11080643

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

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