4nxl

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<StructureSection load='4nxl' size='340' side='right'caption='[[4nxl]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='4nxl' size='340' side='right'caption='[[4nxl]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4nxl]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"mycobacterium_erythropolis"_gray_and_thornton_1928 "mycobacterium erythropolis" gray and thornton 1928]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NXL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NXL FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4nxl]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodococcus_erythropolis Rhodococcus erythropolis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NXL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NXL FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dszC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1833 "Mycobacterium erythropolis" Gray and Thornton 1928])</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]] 2.3&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4nxl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nxl OCA], [http://pdbe.org/4nxl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4nxl RCSB], [http://www.ebi.ac.uk/pdbsum/4nxl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4nxl ProSAT]</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=4nxl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nxl OCA], [https://pdbe.org/4nxl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nxl RCSB], [https://www.ebi.ac.uk/pdbsum/4nxl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nxl 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/DSZC3_RHOER DSZC3_RHOER] Catalyzes the first step of the '4S' desulfurization pathway that removes covalently bound sulfur from dibenzothiophene (DBT) without breaking carbon-carbon bonds. Sulfur dioxygenase which converts DBT to DBT-sulfone (DBTO2 or DBT 5,5-dioxide) in a stepwise manner.<ref>PMID:24975806</ref> <ref>PMID:16810451</ref>
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Dibenzothiophene (DBT) is a typical sulfur-containing compound found in fossil fuels. This compound and its derivatives are resistant to the hydrodesulfurization method often used in industry, but they are susceptible to enzymatic desulfurization via the 4S pathway, which is a well-studied biochemical pathway consisting of four enzymes. DBT monooxygenase (DszC) from Rhodococcus erythropolis is involved in the first step of the 4S pathway. We determined the crystal structure of DszC, which reveals that, in contrast to several homologous proteins, the C-terminus (410-417) of DszC participates in the stabilization of the substrate-binding pocket. Analytical ultracentrifugation analysis and enzymatic assays confirmed that the C-terminus is important for the stabilization of the active conformation of the substrate-binding pocket and the tetrameric state. Therefore, the C-terminus of DszC plays a significant role in the catalytic activity of this enzyme. Proteins 2014. (c) 2014 Wiley Periodicals, Inc.
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Structural insights into the stabilization of active, tetrameric DszC by its C-terminus.,Zhang L, Duan X, Zhou D, Dong Z, Ji K, Meng W, Li G, Li X, Yang H, Ma T, Rao Z Proteins. 2014 Jun 28. doi: 10.1002/prot.24638. PMID:24975806<ref>PMID:24975806</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 4nxl" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Mycobacterium erythropolis gray and thornton 1928]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Duan, X]]
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[[Category: Rhodococcus erythropolis]]
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[[Category: Li, X]]
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[[Category: Duan X]]
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[[Category: Rao, Z]]
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[[Category: Li X]]
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[[Category: Zhang, L]]
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[[Category: Rao Z]]
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[[Category: Monooxygenase]]
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[[Category: Zhang L]]
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[[Category: Oxidoreductase]]
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Current revision

Dibenzothiophene monooxygenase (DszC) from Rhodococcus erythropolis

PDB ID 4nxl

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