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6kue

From Proteopedia

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Current revision (10:44, 27 March 2024) (edit) (undo)
 
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<StructureSection load='6kue' size='340' side='right'caption='[[6kue]], [[Resolution|resolution]] 1.99&Aring;' scene=''>
<StructureSection load='6kue' size='340' side='right'caption='[[6kue]], [[Resolution|resolution]] 1.99&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6kue]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"achromobacter_radiobacter"_(beijerinck_and_van_delden_1902)_bergey_et_al._1934 "achromobacter radiobacter" (beijerinck and van delden 1902) bergey et al. 1934]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KUE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6KUE FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6kue]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Agrobacterium_tumefaciens Agrobacterium tumefaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KUE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6KUE FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SY94_3983 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=358 "Achromobacter radiobacter" (Beijerinck and van Delden 1902) Bergey et al. 1934])</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]] 1.992&#8491;</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/Beta-ketoacyl-[acyl-carrier-protein]_synthase_I Beta-ketoacyl-[acyl-carrier-protein] synthase I], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.41 2.3.1.41] </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=6kue FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kue OCA], [https://pdbe.org/6kue PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6kue RCSB], [https://www.ebi.ac.uk/pdbsum/6kue PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6kue 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=6kue FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kue OCA], [https://pdbe.org/6kue PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6kue RCSB], [https://www.ebi.ac.uk/pdbsum/6kue PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6kue 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/A0A0F4FMM6_RHIRD A0A0F4FMM6_RHIRD]
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Biotin is an essential micro-nutrient across the three domains of life. The paradigm earlier step of biotin synthesis denotes "BioC-BioH" pathway in Escherichia coli. Here we report that BioZ bypasses the canonical route to begin biotin synthesis. In addition to its origin of Rhizobiales, protein phylogeny infers that BioZ is domesticated to gain an atypical role of beta-ketoacyl-ACP synthase III. Genetic and biochemical characterization demonstrates that BioZ catalyzes the condensation of glutaryl-CoA (or ACP) with malonyl-ACP to give 5'-keto-pimeloyl ACP. This intermediate proceeds via type II fatty acid synthesis (FAS II) pathway, to initiate the formation of pimeloyl-ACP, a precursor of biotin synthesis. To further explore molecular basis of BioZ activity, we determine the crystal structure of Agrobacterium tumefaciens BioZ at 1.99 A, of which the catalytic triad and the substrate-loading tunnel are functionally defined. In particular, we localize that three residues (S84, R147, and S287) at the distant bottom of the tunnel might neutralize the charge of free C-carboxyl group of the primer glutaryl-CoA. Taken together, this study provides molecular insights into the BioZ biotin synthesis pathway.
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Biochemical and structural characterization of the BioZ enzyme engaged in bacterial biotin synthesis pathway.,Zhang S, Xu Y, Guan H, Cui T, Liao Y, Wei W, Li J, Hassan BH, Zhang H, Jia X, Ouyang S, Feng Y Nat Commun. 2021 Apr 6;12(1):2056. doi: 10.1038/s41467-021-22360-4. PMID:33824341<ref>PMID:33824341</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 6kue" 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: Agrobacterium tumefaciens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Hongxin, G]]
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[[Category: Hongxin G]]
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[[Category: Ouyang, S]]
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[[Category: Ouyang S]]
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[[Category: Sitao, Z]]
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[[Category: Sitao Z]]
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[[Category: Structure bioz]]
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[[Category: Transferase]]
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Current revision

The structure of BioZ from Agrobacterium tumefaciens

PDB ID 6kue

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