This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1whu

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (13:40, 9 May 2024) (edit) (undo)
 
Line 1: Line 1:
==Solution structure of the alpha-helical domain from mouse hypothetical PNPase==
==Solution structure of the alpha-helical domain from mouse hypothetical PNPase==
-
<StructureSection load='1whu' size='340' side='right'caption='[[1whu]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+
<StructureSection load='1whu' size='340' side='right'caption='[[1whu]]' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[1whu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WHU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WHU FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[1whu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WHU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WHU FirstGlance]. <br>
-
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RIKEN CDNA 1200003F12 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
-
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Polyribonucleotide_nucleotidyltransferase Polyribonucleotide nucleotidyltransferase], with EC number [https://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'>[https://proteopedia.org/fgij/fg.htm?mol=1whu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1whu OCA], [https://pdbe.org/1whu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1whu RCSB], [https://www.ebi.ac.uk/pdbsum/1whu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1whu ProSAT], [https://www.topsan.org/Proteins/RSGI/1whu TOPSAN]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1whu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1whu OCA], [https://pdbe.org/1whu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1whu RCSB], [https://www.ebi.ac.uk/pdbsum/1whu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1whu ProSAT], [https://www.topsan.org/Proteins/RSGI/1whu TOPSAN]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[https://www.uniprot.org/uniprot/PNPT1_MOUSE PNPT1_MOUSE]] RNA-binding protein implicated in numerous RNA metabolic processes. Hydrolyzes single-stranded polyribonucleotides processively in the 3'-to-5' direction. Mitochondrial intermembrane factor with RNA-processing exoribonulease activity. Component of the mitochondrial degradosome (mtEXO) complex, that degrades 3' overhang double-stranded RNA with a 3'-to-5' directionality in an ATP-dependent manner. Required for correct processing and polyadenylation of mitochondrial mRNAs. Plays a role as a cytoplasmic RNA import factor that mediates the translocation of small RNA components, like the 5S RNA, the RNA subunit of ribonuclease P and the mitochondrial RNA-processing (MRP) RNA, into the mitochondrial matrix. Plays a role in mitochondrial morphogenesis and respiration; regulates the expression of the electron transport chain (ETC) components at the mRNA and protein levels. In the cytoplasm, shows a 3'-to-5' exoribonuclease mediating mRNA degradation activity; degrades c-myc mRNA upon treatment with IFNB1/IFN-beta, resulting in a growth arrest in melanoma cells. Regulates the stability of specific mature miRNAs in melanoma cells; specifically and selectively degrades miR-221, preferentially. Plays also a role in RNA cell surveillance by cleaning up oxidized RNAs. Binds to the RNA subunit of ribonuclease P, MRP RNA and miR-221 microRNA.<ref>PMID:20691904</ref>
+
[https://www.uniprot.org/uniprot/PNPT1_MOUSE PNPT1_MOUSE] RNA-binding protein implicated in numerous RNA metabolic processes. Hydrolyzes single-stranded polyribonucleotides processively in the 3'-to-5' direction. Mitochondrial intermembrane factor with RNA-processing exoribonulease activity. Component of the mitochondrial degradosome (mtEXO) complex, that degrades 3' overhang double-stranded RNA with a 3'-to-5' directionality in an ATP-dependent manner. Required for correct processing and polyadenylation of mitochondrial mRNAs. Plays a role as a cytoplasmic RNA import factor that mediates the translocation of small RNA components, like the 5S RNA, the RNA subunit of ribonuclease P and the mitochondrial RNA-processing (MRP) RNA, into the mitochondrial matrix. Plays a role in mitochondrial morphogenesis and respiration; regulates the expression of the electron transport chain (ETC) components at the mRNA and protein levels. In the cytoplasm, shows a 3'-to-5' exoribonuclease mediating mRNA degradation activity; degrades c-myc mRNA upon treatment with IFNB1/IFN-beta, resulting in a growth arrest in melanoma cells. Regulates the stability of specific mature miRNAs in melanoma cells; specifically and selectively degrades miR-221, preferentially. Plays also a role in RNA cell surveillance by cleaning up oxidized RNAs. Binds to the RNA subunit of ribonuclease P, MRP RNA and miR-221 microRNA.<ref>PMID:20691904</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 25: Line 24:
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Lk3 transgenic mice]]
+
[[Category: Mus musculus]]
-
[[Category: Polyribonucleotide nucleotidyltransferase]]
+
[[Category: Inoue M]]
-
[[Category: Inoue, M]]
+
[[Category: Kigawa T]]
-
[[Category: Kigawa, T]]
+
[[Category: Muto Y]]
-
[[Category: Muto, Y]]
+
[[Category: Nagata T]]
-
[[Category: Nagata, T]]
+
[[Category: Shirouzu M]]
-
[[Category: Structural genomic]]
+
[[Category: Terada T]]
-
[[Category: Shirouzu, M]]
+
[[Category: Yokoyama S]]
-
[[Category: Terada, T]]
+
-
[[Category: Yokoyama, S]]
+
-
[[Category: 3'-5' rna exonuclease]]
+
-
[[Category: Alpha-helical domain]]
+
-
[[Category: Pnpase]]
+
-
[[Category: Polynucleotide phosphorylase]]
+
-
[[Category: Rsgi]]
+
-
[[Category: Transferase]]
+

Current revision

Solution structure of the alpha-helical domain from mouse hypothetical PNPase

PDB ID 1whu

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools