3ten

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<StructureSection load='3ten' size='340' side='right'caption='[[3ten]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
<StructureSection load='3ten' size='340' side='right'caption='[[3ten]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3ten]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Acidianus_sp._a1-3 Acidianus sp. a1-3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TEN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TEN FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3ten]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Acidianus_sp._A1-3 Acidianus sp. A1-3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TEN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TEN FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3teo|3teo]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=3ten FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ten OCA], [https://pdbe.org/3ten PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ten RCSB], [https://www.ebi.ac.uk/pdbsum/3ten PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ten ProSAT]</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=3ten FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ten OCA], [https://pdbe.org/3ten PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ten RCSB], [https://www.ebi.ac.uk/pdbsum/3ten PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ten ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/CS2H_ACIS1 CS2H_ACIS1] Catalyzes the conversion of carbon disulfide into hydrogen sulfide and carbon dioxide, with carbonyl sulfide as an intermediate. Likely plays a key role in sulfur metabolism that allows Acidianus sp. A1-3 to grow on carbon disulfide as the main carbon and energy source. Does not show carbonic anhydrase activity (hydration of CO(2) to carbonate).<ref>PMID:22012399</ref>
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Extremophilic organisms require specialized enzymes for their exotic metabolisms. Acid-loving thermophilic Archaea that live in the mudpots of volcanic solfataras obtain their energy from reduced sulphur compounds such as hydrogen sulphide (H(2)S) and carbon disulphide (CS(2)). The oxidation of these compounds into sulphuric acid creates the extremely acidic environment that characterizes solfataras. The hyperthermophilic Acidianus strain A1-3, which was isolated from the fumarolic, ancient sauna building at the Solfatara volcano (Naples, Italy), was shown to rapidly convert CS(2) into H(2)S and carbon dioxide (CO(2)), but nothing has been known about the modes of action and the evolution of the enzyme(s) involved. Here we describe the structure, the proposed mechanism and evolution of a CS(2) hydrolase from Acidianus A1-3. The enzyme monomer displays a typical beta-carbonic anhydrase fold and active site, yet CO(2) is not one of its substrates. Owing to large carboxy- and amino-terminal arms, an unusual hexadecameric catenane oligomer has evolved. This structure results in the blocking of the entrance to the active site that is found in canonical beta-carbonic anhydrases and the formation of a single 15-A-long, highly hydrophobic tunnel that functions as a specificity filter. The tunnel determines the enzyme's substrate specificity for CS(2), which is hydrophobic. The transposon sequences that surround the gene encoding this CS(2) hydrolase point to horizontal gene transfer as a mechanism for its acquisition during evolution. Our results show how the ancient beta-carbonic anhydrase, which is central to global carbon metabolism, was transformed by divergent evolution into a crucial enzyme in CS(2) metabolism.
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Evolution of a new enzyme for carbon disulphide conversion by an acidothermophilic archaeon.,Smeulders MJ, Barends TR, Pol A, Scherer A, Zandvoort MH, Udvarhelyi A, Khadem AF, Menzel A, Hermans J, Shoeman RL, Wessels HJ, van den Heuvel LP, Russ L, Schlichting I, Jetten MS, Op den Camp HJ Nature. 2011 Oct 19;478(7369):412-6. doi: 10.1038/nature10464. PMID:22012399<ref>PMID:22012399</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3ten" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Acidianus sp. a1-3]]
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[[Category: Acidianus sp. A1-3]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Barends, T R.M B]]
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[[Category: Barends TRMB]]
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[[Category: Camp, H J.M Op den]]
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[[Category: Hermans J]]
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[[Category: Hermans, J]]
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[[Category: Jetten MSM]]
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[[Category: Heuvel, L P.van den]]
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[[Category: Khadem A]]
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[[Category: Jetten, M S.M]]
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[[Category: Menzel A]]
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[[Category: Khadem, A]]
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[[Category: Op den Camp HJM]]
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[[Category: Menzel, A]]
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[[Category: Pol A]]
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[[Category: Pol, A]]
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[[Category: Russ L]]
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[[Category: Russ, L]]
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[[Category: Scherer A]]
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[[Category: Scherer, A]]
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[[Category: Schlichting I]]
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[[Category: Schlichting, I]]
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[[Category: Shoeman RL]]
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[[Category: Shoeman, R L]]
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[[Category: Smeulders MJ]]
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[[Category: Smeulders, M J]]
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[[Category: Udvarhelyi A]]
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[[Category: Udvarhelyi, A]]
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[[Category: Wessels HJCT]]
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[[Category: Wessels, H J.C T]]
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[[Category: Zandvoort MH]]
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[[Category: Zandvoort, M H]]
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[[Category: Van den Heuvel LP]]
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[[Category: Beta carbonic anhydrase fold]]
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[[Category: Carbon disulfide hydrolysis]]
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[[Category: Hydrolase]]
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[[Category: None]]
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Current revision

Holo form of carbon disulfide hydrolase

PDB ID 3ten

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