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6ir4
From Proteopedia
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<StructureSection load='6ir4' size='340' side='right'caption='[[6ir4]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='6ir4' size='340' side='right'caption='[[6ir4]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6ir4]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[6ir4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechocystis_sp._PCC_6803 Synechocystis sp. PCC 6803]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IR4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6IR4 FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6ir4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ir4 OCA], [https://pdbe.org/6ir4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ir4 RCSB], [https://www.ebi.ac.uk/pdbsum/6ir4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ir4 ProSAT]</span></td></tr> |
</table> | </table> | ||
| - | + | == Function == | |
| - | = | + | [https://www.uniprot.org/uniprot/BIOU_SYNY3 BIOU_SYNY3] A 'suicide' enzyme that participates in biotin synthesis. Catalyzes the formation of (S)-8-amino-7-oxononanoate (DAN-carbamic acid) from (7R,8S)-8-amino-7-(carboxyamino)nonanoate (DAN), a function equivalent to the cannonical BioA reaction and the first half-reaction of BioD. The cellular requirement for biotin is thought be low enough that this single turnover enzyme supplies a sufficient amount of the cofactor. Overall it catalyzes three reactions: formation of a covalent linkage with 8-amino-7-oxononanoate to yield a BioU-DAN conjugate at the epsilon-amino group of Lys124 of BioU using NAD(P)H, carboxylation of the conjugate to form BioU-DAN-carbamic acid, and release of DAN-carbamic acid using NAD(P)+ (By similarity) (PubMed:32042199). A coupled Synechocystis BioU/BioD assay produces dethiobiotin from DAN. Complements a bioA deletion in E.coli but not a bioD1 deletion (PubMed:32042199).[HAMAP-Rule:MF_00852]<ref>PMID:32042199</ref> |
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== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Kuzuyama | + | [[Category: Synechocystis sp. PCC 6803]] |
| - | [[Category: Nishiyama | + | [[Category: Kuzuyama T]] |
| - | [[Category: Oishi | + | [[Category: Nishiyama M]] |
| - | [[Category: Sakaki | + | [[Category: Oishi K]] |
| - | [[Category: Shimizu | + | [[Category: Sakaki K]] |
| - | [[Category: Tomita | + | [[Category: Shimizu T]] |
| - | + | [[Category: Tomita T]] | |
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Current revision
Crystal structure of BioU from Synechocystis sp.PCC6803 (apo form)
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