View source for 7r37


==Crystal structure of S-adenosyl-L-homocysteine hydrolase from Pyrococcus furiosus in complex with inosine==
<StructureSection load='7r37' size='340' side='right'caption='[[7r37]], [[Resolution|resolution]] 2.28&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7r37]] 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=7R37 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7R37 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]] 2.28&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=NOS:INOSINE'>NOS</scene></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=7r37 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7r37 OCA], [https://pdbe.org/7r37 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7r37 RCSB], [https://www.ebi.ac.uk/pdbsum/7r37 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7r37 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7r37" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pyrococcus furiosus]]
[[Category: Andexer JN]]
[[Category: Popadic D]]
[[Category: Saleem-Batcha R]]