View source for 7rlu


==Structure of ALDH1L1 (10-formyltetrahydrofolate dehydrogenase) in complex with NADP==
<StructureSection load='7rlu' size='340' side='right'caption='[[7rlu]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7rlu]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7RLU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7RLU FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=PNS:4-PHOSPHOPANTETHEINE'>PNS</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[7rlt|7rlt]]</div></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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7rlu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7rlu OCA], [https://pdbe.org/7rlu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7rlu RCSB], [https://www.ebi.ac.uk/pdbsum/7rlu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7rlu ProSAT]</span></td></tr>
</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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7rlu" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Formyltetrahydrofolate dehydrogenase]]
[[Category: Large Structures]]
[[Category: Golczak, M]]
[[Category: Krupenko, N I]]
[[Category: Krupenko, S A]]
[[Category: Sereda, V]]
[[Category: Tsybovsky, Y]]
[[Category: Acyl carrier protein]]
[[Category: Cytosolic protein]]
[[Category: Folate metabolism]]
[[Category: Peptidyl carrier protein]]