3qus

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<StructureSection load='3qus' size='340' side='right'caption='[[3qus]], [[Resolution|resolution]] 2.84&Aring;' scene=''>
<StructureSection load='3qus' size='340' side='right'caption='[[3qus]], [[Resolution|resolution]] 2.84&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3qus]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_35608 Atcc 35608]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QUS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QUS FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3qus]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Moorella_thermoacetica Moorella thermoacetica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QUS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QUS FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene>, <scene name='pdbligand=MAE:MALEIC+ACID'>MAE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TOE:2-[2-(2-METHOXY-ETHOXY)-ETHOXY]-ETHOXYL'>TOE</scene></td></tr>
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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]] 2.84&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3pzx|3pzx]], [[3qb6|3qb6]], [[1eg7|1eg7]], [[1fpm|1fpm]], [[1fp7|1fp7]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene>, <scene name='pdbligand=MAE:MALEIC+ACID'>MAE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TOE:2-[2-(2-METHOXY-ETHOXY)-ETHOXY]-ETHOXYL'>TOE</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fhs, Moorella ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1525 ATCC 35608])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Formate--tetrahydrofolate_ligase Formate--tetrahydrofolate ligase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.4.3 6.3.4.3] </span></td></tr>
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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=3qus FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qus OCA], [https://pdbe.org/3qus PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qus RCSB], [https://www.ebi.ac.uk/pdbsum/3qus PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qus 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=3qus FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qus OCA], [https://pdbe.org/3qus PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qus RCSB], [https://www.ebi.ac.uk/pdbsum/3qus PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qus ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/FTHS_MOOTH FTHS_MOOTH]
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N(10) -formyltetrahydrofolate synthetase (FTHFS) is a folate enzyme that catalyzes the formylation of tetrahydrofolate (THF) in an ATP dependent manner. Structures of FTHFS from the thermophilic homoacetogen, Moorella thermoacetica, complexed with 1) a catalytic intermediate - formylphosphate (XPO) and product - ADP; 2) with an inhibitory substrate analog - folate; 3) with XPO and an inhibitory THF analog, ZD9331, were used to analyze the enzyme mechanism. Nucleophilic attack of the formate ion on the gamma phosphate of ATP leads to the formation of XPO and the first product ADP. A channel that leads to the putative formate binding pocket allows for the binding of ATP and formate in random order. Formate binding is due to interactions with the gamma-phosphate moiety of ATP and additionally to two hydrogen bonds from the backbone nitrogen of Ala276 and the side chain of Arg97. Upon ADP dissociation, XPO reorients and moves to the position previously occupied by the beta-phosphate of ATP. Conformational changes that occur due to the XPO presence apparently allow for the recruitment of the third substrate, THF, with its pterin moiety positioned between Phe384 and Trp412. This position overlaps with that of the bound nucleoside, which is consistent with a catalytic mechanism hypothesis that FTHFS works via a sequential ping-pong mechanism. More specifically, a random bi uni uni bi ping-pong ter ter mechanism is proposed. Additionally, the native structure originally reported at a 2.5 A resolution was redetermined at a 2.2 A resolution.
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Mechanism of N(10) -formyltetrahydrofolate synthetase derived from complexes with intermediates and inhibitors.,Celeste LR, Chai G, Bielak M, Minor W, Lovelace LL, Lebioda L Protein Sci. 2011 Nov 22. doi: 10.1002/pro.2005. PMID:22109967<ref>PMID:22109967</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3qus" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 35608]]
 
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[[Category: Formate--tetrahydrofolate ligase]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Bielak, M]]
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[[Category: Moorella thermoacetica]]
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[[Category: Celeste, L R]]
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[[Category: Bielak M]]
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[[Category: Chai, G]]
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[[Category: Celeste LR]]
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[[Category: Lebioda, L]]
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[[Category: Chai G]]
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[[Category: Lovelace, L L]]
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[[Category: Lebioda L]]
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[[Category: Ligase]]
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[[Category: Lovelace LL]]

Current revision

Crystal Structure of N10-Formyltetrahydrofolate Synthetase with ATPgS

PDB ID 3qus

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