3x2f: Difference between revisions
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==A Thermophilic S-Adenosylhomocysteine Hydrolase== | |||
<StructureSection load='3x2f' size='340' side='right'caption='[[3x2f]], [[Resolution|resolution]] 2.04Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3x2f]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima_MSB8 Thermotoga maritima MSB8]. 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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.04Å</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> | |||
<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> | |||
== Function == | |||
[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] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 3x2f" style="background-color:#fffaf0;"></div> | ||
[[Category: Ko | == References == | ||
[[Category: | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Thermotoga maritima MSB8]] | |||
[[Category: Huang CH]] | |||
[[Category: Ko TP]] | |||
[[Category: Zheng Y]] | |||
Latest revision as of 16:40, 8 November 2023
A Thermophilic S-Adenosylhomocysteine HydrolaseA Thermophilic S-Adenosylhomocysteine Hydrolase
Structural highlights
FunctionSAHH_THEMA May play a key role in the regulation of the intracellular concentration of adenosylhomocysteine.[HAMAP-Rule:MF_00563] Publication Abstract from PubMedS-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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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