3ui5
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | [[ | + | ==Crystal structure of human Parvulin 14== |
| + | <StructureSection load='3ui5' size='340' side='right' caption='[[3ui5]], [[Resolution|resolution]] 1.40Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3ui5]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3UI5 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ui4|3ui4]], [[3ui6|3ui6]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PIN4, Q9Y237 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </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=3ui5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ui5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ui5 RCSB], [http://www.ebi.ac.uk/pdbsum/3ui5 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | ||
| - | == | + | |
| - | < | + | |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Peptidylprolyl isomerase]] | [[Category: Peptidylprolyl isomerase]] | ||
| - | [[Category: Bayer, P | + | [[Category: Bayer, P]] |
| - | [[Category: Blankenfeldt, W | + | [[Category: Blankenfeldt, W]] |
| - | [[Category: Hoppstock, L | + | [[Category: Hoppstock, L]] |
| - | [[Category: Link, N M | + | [[Category: Link, N M]] |
| - | [[Category: Matena, A | + | [[Category: Matena, A]] |
| - | [[Category: Mueller, J W | + | [[Category: Mueller, J W]] |
| - | [[Category: Rueppel, A | + | [[Category: Rueppel, A]] |
[[Category: Isomerase]] | [[Category: Isomerase]] | ||
[[Category: Peptidyl-prolyl-isomerase]] | [[Category: Peptidyl-prolyl-isomerase]] | ||
Revision as of 17:25, 9 December 2014
Crystal structure of human Parvulin 14
| |||||||||||
