6ir4

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (10:34, 27 March 2024) (edit) (undo)
 
(3 intermediate revisions not shown.)
Line 1: Line 1:
-
'''Unreleased structure'''
 
-
The entry 6ir4 is ON HOLD until Paper Publication
+
==Crystal structure of BioU from Synechocystis sp.PCC6803 (apo form)==
-
 
+
<StructureSection load='6ir4' size='340' side='right'caption='[[6ir4]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
-
Authors:
+
== Structural highlights ==
-
 
+
<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>
-
Description:
+
</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&#8491;</td></tr>
-
[[Category: Unreleased Structures]]
+
<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>
 +
== 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>
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Large Structures]]
 +
[[Category: Synechocystis sp. PCC 6803]]
 +
[[Category: Kuzuyama T]]
 +
[[Category: Nishiyama M]]
 +
[[Category: Oishi K]]
 +
[[Category: Sakaki K]]
 +
[[Category: Shimizu T]]
 +
[[Category: Tomita T]]

Current revision

Crystal structure of BioU from Synechocystis sp.PCC6803 (apo form)

PDB ID 6ir4

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools