7rlt: Difference between revisions

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<StructureSection load='7rlt' size='340' side='right'caption='[[7rlt]], [[Resolution|resolution]] 3.70&Aring;' scene=''>
<StructureSection load='7rlt' size='340' side='right'caption='[[7rlt]], [[Resolution|resolution]] 3.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7rlt]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7RLT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7RLT FirstGlance]. <br>
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7RLT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7RLT FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PNS:4-PHOSPHOPANTETHEINE'>PNS</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.7&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Formyltetrahydrofolate_dehydrogenase Formyltetrahydrofolate dehydrogenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.6 1.5.1.6] </span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PNS:4-PHOSPHOPANTETHEINE'>PNS</scene></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=7rlt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7rlt OCA], [https://pdbe.org/7rlt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7rlt RCSB], [https://www.ebi.ac.uk/pdbsum/7rlt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7rlt 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=7rlt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7rlt OCA], [https://pdbe.org/7rlt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7rlt RCSB], [https://www.ebi.ac.uk/pdbsum/7rlt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7rlt ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Putative tumor suppressor ALDH1L1, the product of natural fusion of three unrelated genes, regulates folate metabolism by catalyzing NADP(+)-dependent conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. Cryo-EM structures of tetrameric rat ALDH1L1 revealed the architecture and functional domain interactions of this complex enzyme. Highly mobile N-terminal domains, which remove formyl from 10-formyltetrahydrofolate, undergo multiple transient inter-domain interactions. The C-terminal aldehyde dehydrogenase domains, which convert formyl to CO2, form unusually large interfaces with the intermediate domains, homologs of acyl/peptidyl carrier proteins (A/PCPs), which transfer the formyl group between the catalytic domains. The 4'-phosphopantetheine arm of the intermediate domain is fully extended and reaches deep into the catalytic pocket of the C-terminal domain. Remarkably, the tetrameric state of ALDH1L1 is indispensable for catalysis because the intermediate domain transfers formyl between the catalytic domains of different protomers. These findings emphasize the versatility of A/PCPs in complex, highly dynamic enzymatic systems.


Structure of putative tumor suppressor ALDH1L1.,Tsybovsky Y, Sereda V, Golczak M, Krupenko NI, Krupenko SA Commun Biol. 2022 Jan 10;5(1):3. doi: 10.1038/s42003-021-02963-9. PMID:35013550<ref>PMID:35013550</ref>
==See Also==
 
*[[Aldehyde dehydrogenase 3D structures|Aldehyde dehydrogenase 3D structures]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7rlt" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Formyltetrahydrofolate dehydrogenase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Golczak, M]]
[[Category: Golczak M]]
[[Category: Krupenko, N I]]
[[Category: Krupenko NI]]
[[Category: Krupenko, S A]]
[[Category: Krupenko SA]]
[[Category: Sereda, V]]
[[Category: Sereda V]]
[[Category: Tsybovsky, Y]]
[[Category: Tsybovsky Y]]
[[Category: Acyl carrier protein]]
[[Category: Cytosolic protein]]
[[Category: Folate metabolism]]
[[Category: Peptidyl carrier protein]]

Latest revision as of 08:29, 4 March 2026

Structure of ligand-free ALDH1L1 (10-formyltetrahydrofolate dehydrogenase)

7rlt, resolution 3.70Å

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