1u79: Difference between revisions

Revision as of 22:08, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1u79.png

Template:STRUCTURE 1u79

Crystal structure of AtFKBP13Crystal structure of AtFKBP13

Template:ABSTRACT PUBMED 15356344

About this StructureAbout this Structure

1U79 is a Single protein structure of sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA.

ReferenceReference

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

A chloroplast FKBP interacts with and affects the accumulation of Rieske subunit of cytochrome bf complex., Gupta R, Mould RM, He Z, Luan S, Proc Natl Acad Sci U S A. 2002 Nov 26;99(24):15806-11. Epub 2002 Nov 7. PMID:12424338

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OCA

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-[[Image:1u79.jpg|left|200px]]
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 {{STRUCTURE_1u79|  PDB=1u79  |  SCENE=  }}
-'''Crystal structure of AtFKBP13'''
+===Crystal structure of AtFKBP13===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_15356344}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15356344 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15356344}}
 ==About this Structure==
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 ==Reference==
 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]
+A chloroplast FKBP interacts with and affects the accumulation of Rieske subunit of cytochrome bf complex., Gupta R, Mould RM, He Z, Luan S, Proc Natl Acad Sci U S A. 2002 Nov 26;99(24):15806-11. Epub 2002 Nov 7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12424338 12424338]
 [[Category: Arabidopsis thaliana]]
 [[Category: Peptidylprolyl isomerase]]
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 [[Category: Fk-506 binding protein]]
 [[Category: Tfkbp13]]
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+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 22:08:38 2008''