1e3p: Difference between revisions
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==tungstate derivative of Streptomyces antibioticus PNPase/GPSI enzyme== | ==tungstate derivative of Streptomyces antibioticus PNPase/GPSI enzyme== | ||
<StructureSection load='1e3p' size='340' side='right' caption='[[1e3p]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='1e3p' size='340' side='right'caption='[[1e3p]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1e3p]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"actinomyces_antibioticus"_waksman_and_woodruff_1941 "actinomyces antibioticus" waksman and woodruff 1941]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E3P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E3P FirstGlance]. <br> | <table><tr><td colspan='2'>[[1e3p]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"actinomyces_antibioticus"_waksman_and_woodruff_1941 "actinomyces antibioticus" waksman and woodruff 1941]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E3P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E3P FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=WO4:TUNGSTATE(VI)ION'>WO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=WO4:TUNGSTATE(VI)ION'>WO4</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1e3h|1e3h]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1e3h|1e3h]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat"> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pnp, AFM16_28085 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1890 "Actinomyces antibioticus" Waksman and Woodruff 1941])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Polyribonucleotide_nucleotidyltransferase Polyribonucleotide nucleotidyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.8 2.7.7.8] </span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1e3p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1e3p RCSB], [http://www.ebi.ac.uk/pdbsum/1e3p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1e3p ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1e3p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1e3p RCSB], [http://www.ebi.ac.uk/pdbsum/1e3p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1e3p ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/A0A1S9NJJ0_STRAT A0A1S9NJJ0_STRAT]] Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.[HAMAP-Rule:MF_01595][SAAS:SAAS00360775] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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==See Also== | ==See Also== | ||
*[[Ribonuclease|Ribonuclease]] | |||
*[[Temp|Temp]] | *[[Temp|Temp]] | ||
== References == | == References == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Actinomyces antibioticus waksman and woodruff 1941]] | [[Category: Actinomyces antibioticus waksman and woodruff 1941]] | ||
[[Category: Large Structures]] | |||
[[Category: Polyribonucleotide nucleotidyltransferase]] | |||
[[Category: Jones, G H]] | [[Category: Jones, G H]] | ||
[[Category: Luisi, B F]] | [[Category: Luisi, B F]] | ||
Revision as of 10:00, 6 November 2019
tungstate derivative of Streptomyces antibioticus PNPase/GPSI enzymetungstate derivative of Streptomyces antibioticus PNPase/GPSI enzyme
Structural highlights
Function[A0A1S9NJJ0_STRAT] Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.[HAMAP-Rule:MF_01595][SAAS:SAAS00360775] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedBACKGROUND: 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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