1y0o

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[[Image:1y0o.gif|left|200px]]
 
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{{Structure
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==crystal structure of reduced AtFKBP13==
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|PDB= 1y0o |SIZE=350|CAPTION= <scene name='initialview01'>1y0o</scene>, resolution 1.89&Aring;
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<StructureSection load='1y0o' size='340' side='right'caption='[[1y0o]], [[Resolution|resolution]] 1.89&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1y0o]] 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=1Y0O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y0O FirstGlance]. <br>
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|ACTIVITY= <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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.89&#8491;</td></tr>
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|GENE= AtFKBP13 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 Arabidopsis thaliana])
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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=1y0o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y0o OCA], [https://pdbe.org/1y0o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y0o RCSB], [https://www.ebi.ac.uk/pdbsum/1y0o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y0o ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=[[1u79|1U79]]
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1y0o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y0o OCA], [http://www.ebi.ac.uk/pdbsum/1y0o PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1y0o RCSB]</span>
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[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>
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}}
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/y0/1y0o_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1y0o ConSurf].
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<div style="clear:both"></div>
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'''crystal structure of reduced AtFKBP13'''
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==See Also==
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*[[FKBP 3D structures|FKBP 3D structures]]
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== References ==
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==Overview==
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<references/>
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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.
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__TOC__
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</StructureSection>
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==About this Structure==
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1Y0O is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y0O OCA].
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15356344 15356344]
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[[Category: Arabidopsis thaliana]]
[[Category: Arabidopsis thaliana]]
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[[Category: Peptidylprolyl isomerase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Gayathri G]]
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[[Category: Gayathri, G.]]
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[[Category: Swaminathan K]]
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[[Category: Swaminathan, K.]]
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[[Category: fk-506 binding protein]]
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[[Category: reduced atfkbp13]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:57:16 2008''
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Current revision

crystal structure of reduced AtFKBP13

PDB ID 1y0o

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