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| | <StructureSection load='3ui5' size='340' side='right'caption='[[3ui5]], [[Resolution|resolution]] 1.40Å' scene=''> | | <StructureSection load='3ui5' size='340' side='right'caption='[[3ui5]], [[Resolution|resolution]] 1.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3ui5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UI5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UI5 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3ui5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UI5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UI5 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=D1D:(4S,5S)-1,2-DITHIANE-4,5-DIOL'>D1D</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3ui4|3ui4]], [[3ui6|3ui6]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=D1D:(4S,5S)-1,2-DITHIANE-4,5-DIOL'>D1D</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PIN4, Q9Y237 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </span></td></tr>
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| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ui5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ui5 OCA], [https://pdbe.org/3ui5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ui5 RCSB], [https://www.ebi.ac.uk/pdbsum/3ui5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ui5 ProSAT]</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=3ui5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ui5 OCA], [https://pdbe.org/3ui5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ui5 RCSB], [https://www.ebi.ac.uk/pdbsum/3ui5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ui5 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/PIN4_HUMAN PIN4_HUMAN]] Isoform 1 is involved as a ribosomal RNA processing factor in ribosome biogenesis. Binds to tightly bent AT-rich stretches of double-stranded DNA.<ref>PMID:19369196</ref> Isoform 2 binds to double-stranded DNA.<ref>PMID:19369196</ref>
| + | [https://www.uniprot.org/uniprot/PIN4_HUMAN PIN4_HUMAN] Isoform 1 is involved as a ribosomal RNA processing factor in ribosome biogenesis. Binds to tightly bent AT-rich stretches of double-stranded DNA.<ref>PMID:19369196</ref> Isoform 2 binds to double-stranded DNA.<ref>PMID:19369196</ref> |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | Parvulins compose a family of small peptidyl-prolyl isomerases (PPIases) involved in protein folding and protein quality control. A number of amino acids in the catalytic cavity are highly conserved, but their precise role within the catalytic mechanism is unknown. The 0.8 A crystal structure of the prolyl isomerase domain of parvulin Par14 shows the electron density of hydrogen atoms between the D74, H42, H123, and T118 side chains. This threonine residue has previously not been associated with catalysis, but a corresponding T152A mutant of Pin1 shows a dramatic reduction of catalytic activity without compromising protein stability. The observed catalytic tetrad is strikingly conserved in Pin1- and parvulin-type proteins and hence constitutes a common feature of small peptidyl prolyl isomerases.
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| - | | + | |
| - | Crystallographic Proof for an Extended Hydrogen-Bonding Network in Small Prolyl Isomerases.,Mueller JW, Link NM, Matena A, Hoppstock L, Ruppel A, Bayer P, Blankenfeldt W J Am Chem Soc. 2011 Nov 21. PMID:22081960<ref>PMID:22081960</ref>
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| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 3ui5" style="background-color:#fffaf0;"></div>
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| | | | |
| | ==See Also== | | ==See Also== |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Peptidylprolyl isomerase]]
| + | [[Category: Bayer P]] |
| - | [[Category: Bayer, P]] | + | [[Category: Blankenfeldt W]] |
| - | [[Category: Blankenfeldt, W]] | + | [[Category: Hoppstock L]] |
| - | [[Category: Hoppstock, L]] | + | [[Category: Link NM]] |
| - | [[Category: Link, N M]] | + | [[Category: Matena A]] |
| - | [[Category: Matena, A]] | + | [[Category: Mueller JW]] |
| - | [[Category: Mueller, J W]] | + | [[Category: Rueppel A]] |
| - | [[Category: Rueppel, A]] | + | |
| - | [[Category: Isomerase]]
| + | |
| - | [[Category: Peptidyl-prolyl-isomerase]]
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| Structural highlights
Function
PIN4_HUMAN Isoform 1 is involved as a ribosomal RNA processing factor in ribosome biogenesis. Binds to tightly bent AT-rich stretches of double-stranded DNA.[1] Isoform 2 binds to double-stranded DNA.[2]
See Also
References
- ↑ Fujiyama-Nakamura S, Yoshikawa H, Homma K, Hayano T, Tsujimura-Takahashi T, Izumikawa K, Ishikawa H, Miyazawa N, Yanagida M, Miura Y, Shinkawa T, Yamauchi Y, Isobe T, Takahashi N. Parvulin (Par14), a peptidyl-prolyl cis-trans isomerase, is a novel rRNA processing factor that evolved in the metazoan lineage. Mol Cell Proteomics. 2009 Jul;8(7):1552-65. Epub 2009 Apr 14. PMID:19369196 doi:http://dx.doi.org/M900147-MCP200
- ↑ Fujiyama-Nakamura S, Yoshikawa H, Homma K, Hayano T, Tsujimura-Takahashi T, Izumikawa K, Ishikawa H, Miyazawa N, Yanagida M, Miura Y, Shinkawa T, Yamauchi Y, Isobe T, Takahashi N. Parvulin (Par14), a peptidyl-prolyl cis-trans isomerase, is a novel rRNA processing factor that evolved in the metazoan lineage. Mol Cell Proteomics. 2009 Jul;8(7):1552-65. Epub 2009 Apr 14. PMID:19369196 doi:http://dx.doi.org/M900147-MCP200
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