3auf: Difference between revisions
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==Crystal structure of glycinamide ribonucleotide transformylase 1 from Symbiobacterium toebii== | ==Crystal structure of glycinamide ribonucleotide transformylase 1 from Symbiobacterium toebii== | ||
<StructureSection load='3auf' size='340' side='right' caption='[[3auf]], [[Resolution|resolution]] 2.07Å' scene=''> | <StructureSection load='3auf' size='340' side='right'caption='[[3auf]], [[Resolution|resolution]] 2.07Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3auf]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3auf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"symbiobacterium_toebii"_rhee_et_al._2002 "symbiobacterium toebii" rhee et al. 2002]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AUF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AUF FirstGlance]. <br> | ||
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PurN ([ | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PurN ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=120580 "Symbiobacterium toebii" Rhee et al. 2002])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3auf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3auf OCA], [https://pdbe.org/3auf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3auf RCSB], [https://www.ebi.ac.uk/pdbsum/3auf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3auf ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Symbiobacterium toebii rhee et al. 2002]] | [[Category: Symbiobacterium toebii rhee et al. 2002]] | ||
[[Category: Large Structures]] | |||
[[Category: Baba, S]] | [[Category: Baba, S]] | ||
[[Category: Kanagawa, M]] | [[Category: Kanagawa, M]] | ||
Revision as of 18:04, 29 December 2021
Crystal structure of glycinamide ribonucleotide transformylase 1 from Symbiobacterium toebiiCrystal structure of glycinamide ribonucleotide transformylase 1 from Symbiobacterium toebii
Structural highlights
Publication Abstract from PubMedThe crystal structures of glycinamide ribonucleotide transformylases (PurNs) from Aquifex aeolicus (Aa), Geobacillus kaustophilus (Gk) and Symbiobacterium toebii (St), and of formyltetrahydrofolate hydrolase (PurU) from Thermus thermophilus (Tt) were determined. The monomer structures of the determined PurN and PurU were very similar to the known structure of PurN, but oligomeric states were different; AaPurN and StPurN formed dimers, GkPurN formed monomer and PurU formed tetramer in the crystals. PurU had a regulatory ACT domain in its N-terminal side. So far several structures of PurUs have been determined, yet, the mechanisms of the catalysis and the regulation of PurU have not been elucidated. We, therefore, modelled ligand-bound structures of PurN and PurU, and performed molecular dynamics simulations to elucidate the reaction mechanisms. The evolutionary relationship of the two enzymes is discussed based on the comparisons of the structures and the catalytic mechanisms. Structures and reaction mechanisms of the two related enzymes, PurN and PurU.,Sampei G, Kanagawa M, Baba S, Shimasaki T, Taka H, Mitsui S, Fujiwara S, Yanagida Y, Kusano M, Suzuki S, Terao K, Kawai H, Fukai Y, Nakagawa N, Ebihara A, Kuramitsu S, Yokoyama S, Kawai G J Biochem. 2013 Dec;154(6):569-79. doi: 10.1093/jb/mvt090. Epub 2013 Oct 9. PMID:24108189[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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