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<StructureSection load='3ptj' size='340' side='right'caption='[[3ptj]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
<StructureSection load='3ptj' size='340' side='right'caption='[[3ptj]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3ptj]] is a 1 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=3PTJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PTJ FirstGlance]. <br>
<table><tr><td colspan='2'>[[3ptj]] 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=3PTJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PTJ FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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]] 2.6&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3pvh|3pvh]], [[3pw9|3pw9]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">At1g54780, T22H22.19 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</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=3ptj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ptj OCA], [https://pdbe.org/3ptj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ptj RCSB], [https://www.ebi.ac.uk/pdbsum/3ptj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ptj 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=3ptj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ptj OCA], [https://pdbe.org/3ptj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ptj RCSB], [https://www.ebi.ac.uk/pdbsum/3ptj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ptj ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/U603_ARATH U603_ARATH]
The membrane protein AtTLP18.3 contains a domain of unknown function, DUF477; it forms a polysome with photosynthetic apparatuses in the thylakoid lumen. To explore the molecular function of AtTLP18.3, we resolved its crystal structures with residues 83 to 260, the DUF477 only, and performed a series of biochemical analyses to discover its function. The gene expression of AtTLP18.3 followed a circadian rhythm. X-ray crystallography revealed the folding of AtTLP18.3 as a three-layer sandwich with 3 alpha-helices in the upper layer, 4 beta-sheets in the middle layer, and 2 alpha-helices in the lower layer, which resembles a Rossmann fold. Structural comparison suggested that AtTLP18.3 might be a phosphatase. The enzymatic activity of AtTLP18.3 was further confirmed by phosphatase assay with various substrates (e.g., p-nitrophenyl phosphate, 6,8 difluoro-4-methylumbelliferyl phosphate, O-phospho-L-Serine [pSer] and several synthetic phosphopeptides). Furthermore, we obtained the structure of AtTLP18.3 in complex with pSer to identify the binding site of AtTLP18.3. Our structural and biochemical studies revealed that AtTLP18.3 has a molecular function of a novel acid phosphatase in the thylakoid lumen. DUF477 is accordingly renamed the thylakoid acid phosphatase (TAP) domain.
 
Structural and Functional Assays of AtTLP18.3 Identify Its Novel Acid Phosphatase Activity in Thylakoid Lumen.,Wu HY, Liu MS, Lin TP, Cheng YS Plant Physiol. 2011 Sep 9. PMID:21908686<ref>PMID:21908686</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3ptj" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Arath]]
[[Category: Arabidopsis thaliana]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Cheng, Y S]]
[[Category: Cheng YS]]
[[Category: Lin, T P]]
[[Category: Lin TP]]
[[Category: Liu, M S]]
[[Category: Liu MS]]
[[Category: Wu, H Y]]
[[Category: Wu HY]]
[[Category: Acid phosphatase]]
[[Category: Arabidopsis thaliana thylakoid lumen]]
[[Category: Hydrolase]]
[[Category: Rossmann fold]]
[[Category: Tap domain]]

Revision as of 13:33, 1 March 2024

Structural and functional Analysis of Arabidopsis thaliana thylakoid lumen protein AtTLP18.3

3ptj, resolution 2.60Å

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