2f4e

From Proteopedia

(Difference between revisions)

Current revision

N-terminal domain of FKBP42 from Arabidopsis thaliana

Structural highlights

2f4e is a 2 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.32Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.^[1] ^[2] ^[3] ^[4] ^[5] ^[6]

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 PubMed

We present the three-dimensional structure of the N-terminal FK506-binding protein (FKBP)-like domain of the immunophilin FKBP42 from Arabidopsis thaliana. The data provide the structural background for the explanation of key functional properties reported previously.

Crystal structure of a plant immunophilin domain involved in regulation of MDR-type ABC transporters.,Weiergraber OH, Eckhoff A, Granzin J FEBS Lett. 2006 Jan 9;580(1):251-5. Epub 2005 Dec 12. PMID:16364310^[7]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Geisler M, Kolukisaoglu HU, Bouchard R, Billion K, Berger J, Saal B, Frangne N, Koncz-Kalman Z, Koncz C, Dudler R, Blakeslee JJ, Murphy AS, Martinoia E, Schulz B. TWISTED DWARF1, a unique plasma membrane-anchored immunophilin-like protein, interacts with Arabidopsis multidrug resistance-like transporters AtPGP1 and AtPGP19. Mol Biol Cell. 2003 Oct;14(10):4238-49. Epub 2003 Aug 7. PMID:14517332 doi:http://dx.doi.org/10.1091/mbc.E02-10-0698
↑ Geisler M, Girin M, Brandt S, Vincenzetti V, Plaza S, Paris N, Kobae Y, Maeshima M, Billion K, Kolukisaoglu UH, Schulz B, Martinoia E. Arabidopsis immunophilin-like TWD1 functionally interacts with vacuolar ABC transporters. Mol Biol Cell. 2004 Jul;15(7):3393-405. Epub 2004 May 7. PMID:15133126 doi:http://dx.doi.org/10.1091/mbc.E03-11-0831
↑ Perez-Perez JM, Ponce MR, Micol JL. The ULTRACURVATA2 gene of Arabidopsis encodes an FK506-binding protein involved in auxin and brassinosteroid signaling. Plant Physiol. 2004 Jan;134(1):101-17. PMID:14730066 doi:http://dx.doi.org/10.1104/pp.103.032524
↑ Bouchard R, Bailly A, Blakeslee JJ, Oehring SC, Vincenzetti V, Lee OR, Paponov I, Palme K, Mancuso S, Murphy AS, Schulz B, Geisler M. Immunophilin-like TWISTED DWARF1 modulates auxin efflux activities of Arabidopsis P-glycoproteins. J Biol Chem. 2006 Oct 13;281(41):30603-12. Epub 2006 Aug 3. PMID:16887800 doi:http://dx.doi.org/10.1074/jbc.M604604200
↑ Bailly A, Sovero V, Vincenzetti V, Santelia D, Bartnik D, Koenig BW, Mancuso S, Martinoia E, Geisler M. Modulation of P-glycoproteins by auxin transport inhibitors is mediated by interaction with immunophilins. J Biol Chem. 2008 Aug 1;283(31):21817-26. doi: 10.1074/jbc.M709655200. Epub 2008 , May 22. PMID:18499676 doi:http://dx.doi.org/10.1074/jbc.M709655200
↑ Wu G, Otegui MS, Spalding EP. The ER-localized TWD1 immunophilin is necessary for localization of multidrug resistance-like proteins required for polar auxin transport in Arabidopsis roots. Plant Cell. 2010 Oct;22(10):3295-304. doi: 10.1105/tpc.110.078360. Epub 2010 Oct , 22. PMID:20971896 doi:http://dx.doi.org/10.1105/tpc.110.078360
↑ Weiergraber OH, Eckhoff A, Granzin J. Crystal structure of a plant immunophilin domain involved in regulation of MDR-type ABC transporters. FEBS Lett. 2006 Jan 9;580(1):251-5. Epub 2005 Dec 12. PMID:16364310 doi:10.1016/j.febslet.2005.12.007

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2f4e"

Categories: Arabidopsis thaliana | Large Structures | Eckhoff A | Granzin J | Weiergraber OH

@@ Line 3: / Line 3: @@
 <StructureSection load='2f4e' size='340' side='right'caption='[[2f4e]], [[Resolution|resolution]] 2.32&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2f4e]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F4E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2F4E FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2f4e]] is a 2 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=2F4E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2F4E FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TWD1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</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]] 2.32&#8491;</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=2f4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f4e OCA], [https://pdbe.org/2f4e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2f4e RCSB], [https://www.ebi.ac.uk/pdbsum/2f4e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2f4e ProSAT]</span></td></tr>
 </table>
+== 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 ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 33: / Line 35: @@
 __TOC__
 </StructureSection>
-[[Category: Arath]]
+[[Category: Arabidopsis thaliana]]
 [[Category: Large Structures]]
-[[Category: Eckhoff, A]]
+[[Category: Eckhoff A]]
-[[Category: Granzin, J]]
+[[Category: Granzin J]]
-[[Category: Weiergraber, O H]]
+[[Category: Weiergraber OH]]
-[[Category: Alpha-beta]]
-[[Category: Fkbp-like]]
-[[Category: Signaling protein]]

2f4e

From Proteopedia

Current revision

N-terminal domain of FKBP42 from Arabidopsis thaliana

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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