2if4
From Proteopedia
(Difference between revisions)
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<StructureSection load='2if4' size='340' side='right'caption='[[2if4]], [[Resolution|resolution]] 2.85Å' scene=''> | <StructureSection load='2if4' size='340' side='right'caption='[[2if4]], [[Resolution|resolution]] 2.85Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2if4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[2if4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IF4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IF4 FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.85Å</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=2if4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2if4 OCA], [https://pdbe.org/2if4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2if4 RCSB], [https://www.ebi.ac.uk/pdbsum/2if4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2if4 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=2if4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2if4 OCA], [https://pdbe.org/2if4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2if4 RCSB], [https://www.ebi.ac.uk/pdbsum/2if4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2if4 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/FKB42_ARATH FKB42_ARATH] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity). Modulates the uptake of MRP substrates into the vacuole; reduces metolachlor-GS (MOC-GS) and enhances 17-beta-estradiol 17-(beta-D-glucuronide) (E(2)17betaG) uptake. Regulates cell elongation and orientation. Functions as a positive regulator of PGP1-mediated auxin transport. Confers drug modulation of PGP1 efflux activity as interaction with NPA or flavonol quercetin prevents its physical and functional interaction with PGP1. Required for the proper localization of auxin-related ABCB transporters. Plays a role in brassinosteroid (BR) signaling pathway.<ref>PMID:14517332</ref> <ref>PMID:15133126</ref> <ref>PMID:14730066</ref> <ref>PMID:16887800</ref> <ref>PMID:18499676</ref> <ref>PMID:20971896</ref> | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2if4 ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2if4 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | FKBP42 is a membrane-anchored immunophilin playing a critical role in morphogenesis and development of higher plants. We present the X-ray structure of the cytoplasmic portion of FKBP42 comprising both the FKBP-like domain and the TPR domain at 2.85 A resolution. The data shed light on the probable binding modes of key interaction partners, including HSP90 and two classes of ABC transporters. The resulting models provide a structural background for further investigation of the unique biological properties of this protein. | ||
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| - | Crystal structure of a multi-domain immunophilin from Arabidopsis thaliana: a paradigm for regulation of plant ABC transporters.,Granzin J, Eckhoff A, Weiergraber OH J Mol Biol. 2006 Dec 8;364(4):799-809. Epub 2006 Sep 26. PMID:17045295<ref>PMID:17045295</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 2if4" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Arabidopsis thaliana]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Eckhoff | + | [[Category: Eckhoff A]] |
| - | [[Category: Granzin | + | [[Category: Granzin J]] |
| - | [[Category: Weiergraeber | + | [[Category: Weiergraeber OH]] |
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Current revision
Crystal structure of a multi-domain immunophilin from Arabidopsis thaliana
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