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| | <StructureSection load='6j26' size='340' side='right'caption='[[6j26]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='6j26' size='340' side='right'caption='[[6j26]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6j26]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrococcus_kodakaraensis_(strain_kod1) Pyrococcus kodakaraensis (strain kod1)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6J26 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6J26 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6j26]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermococcus_kodakarensis_KOD1 Thermococcus kodakarensis KOD1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6J26 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6J26 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=B5L:N~1~,N~1~,N~1~-tris(3-azaniumylpropyl)butane-1,4-diaminium'>B5L</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=MTA:5-DEOXY-5-METHYLTHIOADENOSINE'>MTA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">bpsA, TK1691 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=69014 Pyrococcus kodakaraensis (strain KOD1)])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=B5L:N~1~,N~1~,N~1~-tris(3-azaniumylpropyl)butane-1,4-diaminium'>B5L</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=MTA:5-DEOXY-5-METHYLTHIOADENOSINE'>MTA</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.128 2.5.1.128] </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=6j26 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6j26 OCA], [https://pdbe.org/6j26 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6j26 RCSB], [https://www.ebi.ac.uk/pdbsum/6j26 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6j26 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6j26 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6j26 OCA], [http://pdbe.org/6j26 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6j26 RCSB], [http://www.ebi.ac.uk/pdbsum/6j26 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6j26 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/BPSA_THEKO BPSA_THEKO]] Involved in the biosynthesis of branched-chain polyamines, which support the growth of thermophiles under high-temperature conditions. Catalyzes the sequential condensation of spermidine with the aminopropyl groups of decarboxylated S-adenosylmethionines to produce N(4)-bis(aminopropyl)spermidine via N(4)-aminopropylspermidine. Can also use spermine to produce N(4)-aminopropylspermine.<ref>PMID:24610711</ref> | + | [https://www.uniprot.org/uniprot/BPSA_THEKO BPSA_THEKO] Involved in the biosynthesis of branched-chain polyamines, which support the growth of thermophiles under high-temperature conditions. Catalyzes the sequential condensation of spermidine with the aminopropyl groups of decarboxylated S-adenosylmethionines to produce N(4)-bis(aminopropyl)spermidine via N(4)-aminopropylspermidine. Can also use spermine to produce N(4)-aminopropylspermine.<ref>PMID:24610711</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6j26" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6j26" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Spermidine synthase 3D structures|Spermidine synthase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Transferase]] | + | [[Category: Thermococcus kodakarensis KOD1]] |
| - | [[Category: Fujita, J]] | + | [[Category: Fujita J]] |
| - | [[Category: Inoue, T]] | + | [[Category: Inoue T]] |
| - | [[Category: Mizohata, E]] | + | [[Category: Mizohata E]] |
| - | [[Category: Toyoda, M]] | + | [[Category: Toyoda M]] |
| - | [[Category: Branched polyamine]]
| + | |
| - | [[Category: Polyamine biosynthesis]]
| + | |
| - | [[Category: Spermidine]]
| + | |
| Structural highlights
Function
BPSA_THEKO Involved in the biosynthesis of branched-chain polyamines, which support the growth of thermophiles under high-temperature conditions. Catalyzes the sequential condensation of spermidine with the aminopropyl groups of decarboxylated S-adenosylmethionines to produce N(4)-bis(aminopropyl)spermidine via N(4)-aminopropylspermidine. Can also use spermine to produce N(4)-aminopropylspermine.[1]
Publication Abstract from PubMed
Branched-chain polyamine synthase (BpsA) catalyzes sequential aminopropyl transfer from the donor, decarboxylated S-adenosylmethionine (dcSAM), to the acceptor, linear-chain polyamine, resulting in the production of a quaternary-branched polyamine via tertiary branched polyamine intermediates. Here, we analyzed the catalytic properties and X-ray crystal structure of Tth-BpsA from Thermus thermophilus and compared them with those of Tk-BpsA from Thermococcus kodakarensis, which revealed differences in acceptor substrate specificity and C-terminal structure between these two enzymes. To investigate the role of the C-terminal flexible region in acceptor recognition, a region (QDEEATTY) in Tth-BpsA was replaced with that in Tk-BpsA (YDDEESSTT) to create chimeric Tth-BpsA C9, which showed a severe reduction in catalytic efficiency toward N(4) -aminopropylnorspermidine, but not toward N(4) -aminopropylspermidine, mimicking Tk-BpsA substrate specificity. Tth-BpsA C9 Tyr(346) and Thr(354) contributed to discrimination between tertiary branched-chain polyamine substrates, suggesting that the C-terminal region of BpsA recognizes acceptor substrates. Liquid chromatography-tandem mass spectrometry analysis on a Tk-BpsA reaction mixture with dcSAM revealed two aminopropyl groups bound to two of five aspartate/glutamate residues (Glu(339) , Asp(342) , Asp(343) , Glu(344) , and Glu(345) ) in the C-terminal flexible region. Mutating each of these five amino acid residues to asparagine/glutamine resulted in a slight decrease in activity. The quadruple mutant D342N/D343N/E344Q/E345Q exhibited a severe reduction in catalytic efficiency, suggesting that these aspartate/glutamate residues function to receive aminopropyl chains. In addition, the X-ray crystal structure of the Tk-BpsA ternary complex bound to N(4) -bis(aminopropyl)spermidine revealed that Asp(126) and Glu(259) interacted with the aminopropyl moiety in N(4) -aminopropylspermidine.
The C-terminal flexible region of branched-chain polyamine synthase facilitates substrate specificity and catalysis.,Hidese R, Toyoda M, Yoshino KI, Fukuda W, Wihardja GA, Kimura S, Fujita J, Niitsu M, Oshima T, Imanaka T, Mizohata E, Fujiwara S FEBS J. 2019 Jun 4. doi: 10.1111/febs.14949. PMID:31162806[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Okada K, Hidese R, Fukuda W, Niitsu M, Takao K, Horai Y, Umezawa N, Higuchi T, Oshima T, Yoshikawa Y, Imanaka T, Fujiwara S. Identification of a novel aminopropyltransferase involved in the synthesis of branched-chain polyamines in hyperthermophiles. J Bacteriol. 2014 May;196(10):1866-76. doi: 10.1128/JB.01515-14. Epub 2014 Mar 7. PMID:24610711 doi:http://dx.doi.org/10.1128/JB.01515-14
- ↑ Hidese R, Toyoda M, Yoshino KI, Fukuda W, Wihardja GA, Kimura S, Fujita J, Niitsu M, Oshima T, Imanaka T, Mizohata E, Fujiwara S. The C-terminal flexible region of branched-chain polyamine synthase facilitates substrate specificity and catalysis. FEBS J. 2019 Jun 4. doi: 10.1111/febs.14949. PMID:31162806 doi:http://dx.doi.org/10.1111/febs.14949
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