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1e3p
From Proteopedia
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| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 15:04:59 2007'' |
Revision as of 13:00, 30 October 2007
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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 ... [(full description)]
About this Structure
1E3P is a [Single protein] structure of sequence from [Streptomyces antibioticus] with SO4 and WO4 as [ligands]. Structure known Active Site: WO4. 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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