8qno: Difference between revisions
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==Crystal structure of S-adenosyl-L-homocysteine hydrolase treated at 368 K from Pyrococcus furiosus in complex with inosine== | |||
<StructureSection load='8qno' size='340' side='right'caption='[[8qno]], [[Resolution|resolution]] 2.03Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8qno]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8QNO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8QNO 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]] 2.033Å</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=8qno FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8qno OCA], [https://pdbe.org/8qno PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8qno RCSB], [https://www.ebi.ac.uk/pdbsum/8qno PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8qno ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/SAHH_PYRFU SAHH_PYRFU] May play a key role in the regulation of the intracellular concentration of adenosylhomocysteine.[HAMAP-Rule:MF_00563] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
S-Adenosyl-L-homocysteine hydrolase (SAHH) reversibly cleaves S-adenosyl-L-homocysteine, the product of S-adenosyl-L-methionine-dependent methylation reactions. The conversion of S-adenosyl-L-homocysteine into adenosine and L-homocysteine plays an important role in the regulation of the methyl cycle. An alternative metabolic route for S-adenosyl-L-methionine regeneration in the extremophiles Methanocaldococcus jannaschii and Thermotoga maritima has been identified, featuring the deamination of S-adenosyl-L-homocysteine to S-inosyl-L-homocysteine. Herein, we report the structural characterisation of different archaeal SAHHs together with a biochemical analysis of various SAHHs from all three domains of life. Homologues deriving from the Euryarchaeota phylum show a higher conversion rate with S-inosyl-L-homocysteine compared to S-adenosyl-L-homocysteine. Crystal structures of SAHH originating from Pyrococcus furiosus in complex with SLH and inosine as ligands, show architectural flexibility in the active site and offer deeper insights into the binding mode of hypoxanthine-containing substrates. Altogether, the findings of our study support the understanding of an alternative metabolic route for S-adenosyl-L-methionine and offer insights into the evolutionary progression and diversification of SAHHs involved in methyl and purine salvage pathways. | |||
Structure, function and substrate preferences of archaeal S-adenosyl-L-homocysteine hydrolases.,Koeppl LH, Popadic D, Saleem-Batcha R, Germer P, Andexer JN Commun Biol. 2024 Mar 29;7(1):380. doi: 10.1038/s42003-024-06078-9. PMID:38548921<ref>PMID:38548921</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 8qno" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Pyrococcus furiosus]] | |||
[[Category: Andexer JN]] | |||
[[Category: Koeppl LH]] | |||
[[Category: Popadic D]] | |||
[[Category: Saleem-Batcha R]] | |||
Latest revision as of 16:06, 21 August 2024
Crystal structure of S-adenosyl-L-homocysteine hydrolase treated at 368 K from Pyrococcus furiosus in complex with inosineCrystal structure of S-adenosyl-L-homocysteine hydrolase treated at 368 K from Pyrococcus furiosus in complex with inosine
Structural highlights
FunctionSAHH_PYRFU May play a key role in the regulation of the intracellular concentration of adenosylhomocysteine.[HAMAP-Rule:MF_00563] Publication Abstract from PubMedS-Adenosyl-L-homocysteine hydrolase (SAHH) reversibly cleaves S-adenosyl-L-homocysteine, the product of S-adenosyl-L-methionine-dependent methylation reactions. The conversion of S-adenosyl-L-homocysteine into adenosine and L-homocysteine plays an important role in the regulation of the methyl cycle. An alternative metabolic route for S-adenosyl-L-methionine regeneration in the extremophiles Methanocaldococcus jannaschii and Thermotoga maritima has been identified, featuring the deamination of S-adenosyl-L-homocysteine to S-inosyl-L-homocysteine. Herein, we report the structural characterisation of different archaeal SAHHs together with a biochemical analysis of various SAHHs from all three domains of life. Homologues deriving from the Euryarchaeota phylum show a higher conversion rate with S-inosyl-L-homocysteine compared to S-adenosyl-L-homocysteine. Crystal structures of SAHH originating from Pyrococcus furiosus in complex with SLH and inosine as ligands, show architectural flexibility in the active site and offer deeper insights into the binding mode of hypoxanthine-containing substrates. Altogether, the findings of our study support the understanding of an alternative metabolic route for S-adenosyl-L-methionine and offer insights into the evolutionary progression and diversification of SAHHs involved in methyl and purine salvage pathways. Structure, function and substrate preferences of archaeal S-adenosyl-L-homocysteine hydrolases.,Koeppl LH, Popadic D, Saleem-Batcha R, Germer P, Andexer JN Commun Biol. 2024 Mar 29;7(1):380. doi: 10.1038/s42003-024-06078-9. PMID:38548921[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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