8iyi
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Spermidine synthase from Kluyveromyces lactis== | |
| + | <StructureSection load='8iyi' size='340' side='right'caption='[[8iyi]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8iyi]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Kluyveromyces_lactis_NRRL_Y-1140 Kluyveromyces lactis NRRL Y-1140]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8IYI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8IYI FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</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=8iyi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8iyi OCA], [https://pdbe.org/8iyi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8iyi RCSB], [https://www.ebi.ac.uk/pdbsum/8iyi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8iyi ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q6CVU4_KLULA Q6CVU4_KLULA] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Spermidine is a polyamine molecule that performs various cellular functions, such as DNA and RNA stabilization, autophagy modulation, and eIF5A formation, and is generated from putrescine by aminopropyltransferase spermidine synthase (SpdS). During synthesis, the aminopropyl moiety is donated from decarboxylated S-adenosylmethionine to form putrescine, with 5'-deoxy-5'-methylthioadenosine being produced as a byproduct. Although the molecular mechanism of SpdS function has been well-established, its structure-based evolutionary relationships remain to be fully understood. Moreover, only a few structural studies have been conducted on SpdS from fungal species. Here, we determined the crystal structure of an apo-form of SpdS from Kluyveromyces lactis (KlSpdS) at 1.9 A resolution. Structural comparison with its homologs revealed a conformational change in the alpha6 helix linked to the gate-keeping loop, with approximately 40 degrees outward rotation. This change caused the catalytic residue Asp170 to move outward, possibly due to the absence of a ligand in the active site. These findings improve our understanding of the structural diversity of SpdS and provide a missing link that expands our knowledge of the structural features of SpdS in fungal species. | ||
| - | + | Structural Analysis of Spermidine Synthase from Kluyveromyces lactis.,Kim S, Chang JH Molecules. 2023 Apr 13;28(8):3446. doi: 10.3390/molecules28083446. PMID:37110680<ref>PMID:37110680</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 8iyi" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Kluyveromyces lactis NRRL Y-1140]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Chang JH]] | ||
| + | [[Category: Kim S]] | ||
Revision as of 21:21, 28 June 2023
Spermidine synthase from Kluyveromyces lactis
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