3s2y

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<StructureSection load='3s2y' size='340' side='right'caption='[[3s2y]], [[Resolution|resolution]] 2.24&Aring;' scene=''>
<StructureSection load='3s2y' size='340' side='right'caption='[[3s2y]], [[Resolution|resolution]] 2.24&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3s2y]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Acetobacter_sp._lmg_1524 Acetobacter sp. lmg 1524]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3S2Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3S2Y FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3s2y]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Komagataeibacter_hansenii_ATCC_23769 Komagataeibacter hansenii ATCC 23769]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3S2Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3S2Y 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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</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]] 2.244&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GXY_09224 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=714995 Acetobacter sp. LMG 1524])</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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</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=3s2y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s2y OCA], [https://pdbe.org/3s2y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3s2y RCSB], [https://www.ebi.ac.uk/pdbsum/3s2y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3s2y 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=3s2y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s2y OCA], [https://pdbe.org/3s2y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3s2y RCSB], [https://www.ebi.ac.uk/pdbsum/3s2y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3s2y 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/D5QFC5_NOVHA D5QFC5_NOVHA]
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Environmental protection through biological mechanisms that aid in the reductive immobilization of toxic metals (e.g., chromate and uranyl) has been identified to involve specific NADH-dependent flavoproteins that promote cell viability. To understand the enzyme mechanisms responsible for metal reduction, the enzyme kinetics of a putative chromate reductase from Gluconacetobacter hansenii (Gh-ChrR) was measured and the crystal structure of the protein determined at 2.25 A resolution. Gh-ChrR catalyzes the NADH-dependent reduction of chromate, ferricyanide, and uranyl anions under aerobic conditions. Kinetic measurements indicate that NADH acts as a substrate inhibitor; catalysis requires chromate binding prior to NADH association. The crystal structure of Gh-ChrR shows the protein is a homotetramer with one bound flavin mononucleotide (FMN) per subunit. A bound anion is visualized proximal to the FMN at the interface between adjacent subunits within a cationic pocket, which is positioned at an optimal distance for hydride transfer. Site-directed substitutions of residues proposed to involve in both NADH and metal anion binding (N85A or R101A) result in 90-95% reductions in enzyme efficiencies for NADH-dependent chromate reduction. In comparison site-directed substitution of a residue (S118A) participating in the coordination of FMN in the active site results in only modest (50%) reductions in catalytic efficiencies, consistent with the presence of a multitude of side chains that position the FMN in the active site. The proposed proximity relationships between metal anion binding site and enzyme cofactors is discussed in terms of rational design principles for the use of enzymes in chromate and uranyl bioremediation.
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Structure Determination and Functional Analysis of a Chromate Reductase from Gluconacetobacter hansenii.,Jin H, Zhang Y, Buchko GW, Varnum SM, Robinson H, Squier TC, Long PE PLoS One. 2012;7(8):e42432. Epub 2012 Aug 6. PMID:22879982<ref>PMID:22879982</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 3s2y" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Acetobacter sp. lmg 1524]]
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[[Category: Komagataeibacter hansenii ATCC 23769]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Buchko, G W]]
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[[Category: Buchko GW]]
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[[Category: Jin, H]]
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[[Category: Jin H]]
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[[Category: Li, P]]
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[[Category: Li P]]
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[[Category: Long, P E]]
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[[Category: Long PE]]
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[[Category: Robinson, H]]
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[[Category: Robinson H]]
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[[Category: Squier, T C]]
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[[Category: Squier TC]]
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[[Category: Varnum, S M]]
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[[Category: Varnum SM]]
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[[Category: Zhang, Y]]
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[[Category: Zhang Y]]
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[[Category: Chromate reductase]]
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[[Category: Oxidoreductase]]
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[[Category: Uranium reductase]]
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Current revision

Crystal structure of a chromate/uranium reductase from Gluconacetobacter hansenii

PDB ID 3s2y

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