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| | ==Crystal structure of AtFKBP13== | | ==Crystal structure of AtFKBP13== |
| - | <StructureSection load='1u79' size='340' side='right' caption='[[1u79]], [[Resolution|resolution]] 1.85Å' scene=''> | + | <StructureSection load='1u79' size='340' side='right'caption='[[1u79]], [[Resolution|resolution]] 1.85Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1u79]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U79 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1U79 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1u79]] is a 5 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=1U79 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1U79 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AtFKBP13 ([http://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]] 1.85Å</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'>[https://proteopedia.org/fgij/fg.htm?mol=1u79 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u79 OCA], [https://pdbe.org/1u79 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1u79 RCSB], [https://www.ebi.ac.uk/pdbsum/1u79 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1u79 ProSAT]</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=1u79 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u79 OCA], [http://pdbe.org/1u79 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1u79 RCSB], [http://www.ebi.ac.uk/pdbsum/1u79 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1u79 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/FKB13_ARATH FKB13_ARATH]] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Responsive of the major PPIase activity in the chloroplast thylakoid lumen. Regulates the accumulation of Rieske protein, an essential component of the photosynthetic electron transport chain.<ref>PMID:16765949</ref> <ref>PMID:17655280</ref> <ref>PMID:19717822</ref> | + | [https://www.uniprot.org/uniprot/FKB13_ARATH FKB13_ARATH] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Responsive of the major PPIase activity in the chloroplast thylakoid lumen. Regulates the accumulation of Rieske protein, an essential component of the photosynthetic electron transport chain.<ref>PMID:16765949</ref> <ref>PMID:17655280</ref> <ref>PMID:19717822</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/u7/1u79_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/u7/1u79_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | ==See Also== | | ==See Also== |
| - | *[[FK506 binding protein|FK506 binding protein]] | + | *[[FKBP 3D structures|FKBP 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Arath]] | + | [[Category: Arabidopsis thaliana]] |
| - | [[Category: Peptidylprolyl isomerase]] | + | [[Category: Large Structures]] |
| - | [[Category: Gopalan, G]] | + | [[Category: Gopalan G]] |
| - | [[Category: Swaminathan, K]] | + | [[Category: Swaminathan K]] |
| - | [[Category: Fk-506 binding protein]]
| + | |
| - | [[Category: Isomerase]]
| + | |
| - | [[Category: Tfkbp13]]
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| Structural highlights
Function
FKB13_ARATH PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Responsive of the major PPIase activity in the chloroplast thylakoid lumen. Regulates the accumulation of Rieske protein, an essential component of the photosynthetic electron transport chain.[1] [2] [3]
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
Change in redox status has long been known to link light to the posttranslational regulation of chloroplast enzymes. So far, studies have been conducted primarily with thioredoxin-linked members of the stroma that function in a broad array of biosynthetic and degradatory processes. Consequently, little is known about the role of redox in regulating the growing number of enzymes found to occur in the lumen, the site of oxygen evolution in thylakoid membranes. To help fill this gap, we have studied AtFKBP13, an FKBP-type immunophilin earlier shown to interact with a redox-active protein of the lumen, and found the enzyme to contain a pair of disulfide bonds in x-ray structural studies. These disulfides, which in protein mutagenesis experiments were shown to be essential for the associated peptidyl-prolyl isomerase activity, are unique to chloroplast FKBPs and are absent in animal and yeast counterparts. Both disulfide bonds were redox-active and were reduced by thioredoxin from either chloroplast or bacterial sources in a reaction that led to loss of enzyme activity. The results suggest a previously unrecognized paradigm for redox regulation in chloroplasts in which activation by light is achieved in concert with oxygen evolution by the oxidation of sulfhydryl groups (conversion of SH to S-S). Such a mechanism, occurring in the thylakoid lumen, is in direct contrast to regulation of enzymes in the stroma, where reduction of disulfides targeted by thioredoxin (S-S converted to SH) leads to an increase in activity in the light.
Structural analysis uncovers a role for redox in regulating FKBP13, an immunophilin of the chloroplast thylakoid lumen.,Gopalan G, He Z, Balmer Y, Romano P, Gupta R, Heroux A, Buchanan BB, Swaminathan K, Luan S Proc Natl Acad Sci U S A. 2004 Sep 21;101(38):13945-50. Epub 2004 Sep 8. PMID:15356344[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Shapiguzov A, Edvardsson A, Vener AV. Profound redox sensitivity of peptidyl-prolyl isomerase activity in Arabidopsis thylakoid lumen. FEBS Lett. 2006 Jun 26;580(15):3671-6. PMID:16765949 doi:http://dx.doi.org/10.1016/j.febslet.2006.05.054
- ↑ Edvardsson A, Shapiguzov A, Petersson UA, Schroder WP, Vener AV. Immunophilin AtFKBP13 sustains all peptidyl-prolyl isomerase activity in the thylakoid lumen from Arabidopsis thaliana deficient in AtCYP20-2. Biochemistry. 2007 Aug 21;46(33):9432-42. Epub 2007 Jul 27. PMID:17655280 doi:http://dx.doi.org/10.1021/bi700426q
- ↑ Ingelsson B, Shapiguzov A, Kieselbach T, Vener AV. Peptidyl-prolyl isomerase activity in chloroplast thylakoid lumen is a dispensable function of immunophilins in Arabidopsis thaliana. Plant Cell Physiol. 2009 Oct;50(10):1801-14. doi: 10.1093/pcp/pcp122. Epub 2009, Aug 28. PMID:19717822 doi:http://dx.doi.org/10.1093/pcp/pcp122
- ↑ Gopalan G, He Z, Balmer Y, Romano P, Gupta R, Heroux A, Buchanan BB, Swaminathan K, Luan S. Structural analysis uncovers a role for redox in regulating FKBP13, an immunophilin of the chloroplast thylakoid lumen. Proc Natl Acad Sci U S A. 2004 Sep 21;101(38):13945-50. Epub 2004 Sep 8. PMID:15356344 doi:10.1073/pnas.0405240101
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