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| ==A Thermophilic S-Adenosylhomocysteine Hydrolase== | | ==A Thermophilic S-Adenosylhomocysteine Hydrolase== |
| <StructureSection load='3x2f' size='340' side='right'caption='[[3x2f]], [[Resolution|resolution]] 2.04Å' scene=''> | | <StructureSection load='3x2f' size='340' side='right'caption='[[3x2f]]' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[3x2f]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3X2F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3X2F FirstGlance]. <br> | | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3X2F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3X2F FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr> | | </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=3x2f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3x2f OCA], [https://pdbe.org/3x2f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3x2f RCSB], [https://www.ebi.ac.uk/pdbsum/3x2f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3x2f ProSAT]</span></td></tr> |
| <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3x2e|3x2e]]</div></td></tr>
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| <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Adenosylhomocysteinase Adenosylhomocysteinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.3.1.1 3.3.1.1] </span></td></tr>
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| <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3x2f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3x2f OCA], [https://pdbe.org/3x2f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3x2f RCSB], [https://www.ebi.ac.uk/pdbsum/3x2f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3x2f ProSAT]</span></td></tr> | |
| </table> | | </table> |
| == Function ==
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| [[https://www.uniprot.org/uniprot/SAHH_THEMA SAHH_THEMA]] May play a key role in the regulation of the intracellular concentration of adenosylhomocysteine.[HAMAP-Rule:MF_00563]
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| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| S-adenosylhomocysteine (SAH) hydrolase catalyzes the reversible hydrolysis of SAH into adenosine and homocysteine by using NAD(+) as a cofactor. The enzyme from Thermotoga maritima (tmSAHH) has great potentials in industrial applications because of its hyperthermophilic properties. Here, two crystal structures of tmSAHH in complex with NAD(+) show both open and closed conformations despite the absence of bound substrate. Each subunit of the tetrameric enzyme is composed of three domains, namely the catalytic domain, the NAD(+)-binding domain and the C-terminal domain. The NAD(+) binding mode is clearly observed and a substrate analogue can also be modeled into the active site, where two cysteine residues in mesophilic enzymes are replaced by serine and threonine in tmSAHH. Notably, the C-terminal domain of tmSAHH lacks the second loop region of mesophilic SAHH, which is important in NAD(+) binding, and thus exposes the bound cofactor to the solvent. The difference explains the higher NAD(+) requirement of tmSAHH because of the reduced affinity. Furthermore, the feature of missing loop is consistently observed in thermophilic bacterial and archaeal SAHHs, and may be related to their thermostability.
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| Crystal structures of S-adenosylhomocysteine hydrolase from the thermophilic bacterium Thermotoga maritima.,Zheng Y, Chen CC, Ko TP, Xiao X, Yang Y, Huang CH, Qian G, Shao W, Guo RT J Struct Biol. 2015 May;190(2):135-42. doi: 10.1016/j.jsb.2015.03.002. Epub 2015 , Mar 17. PMID:25791616<ref>PMID:25791616</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 3x2f" style="background-color:#fffaf0;"></div>
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| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Adenosylhomocysteinase]]
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| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Huang, C H]] | | [[Category: Huang CH]] |
| [[Category: Ko, T P]] | | [[Category: Ko TP]] |
| [[Category: Zheng, Y]] | | [[Category: Zheng Y]] |
| [[Category: Hydrolase]]
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| [[Category: Nad+ binding]]
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