View source for 4irn


==Crystal Structure of the Prolyl Acyl Carrier Protein Oxidase AnaB==
<StructureSection load='4irn' size='340' side='right'caption='[[4irn]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4irn]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Kamptonema_sp._PCC_6506 Kamptonema sp. PCC 6506]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IRN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IRN FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</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=4irn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4irn OCA], [https://pdbe.org/4irn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4irn RCSB], [https://www.ebi.ac.uk/pdbsum/4irn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4irn ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/C4NCB7_9CYAN C4NCB7_9CYAN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Anatoxin-a and homoanatoxin-a are two potent cyanobacterial neurotoxins biosynthesized from L-proline by a short pathway involving polyketide synthases. Proline is first loaded onto AnaD, an acyl carrier protein, and prolyl-AnaD is then oxidized to 1-pyrroline-5-carboxyl-AnaD by a flavoprotein, AnaB. Three polyketide synthases then transform this imine into anatoxin-a or homoanatoxin-a. AnaB was crystallized in its holo form and its three-dimensional structure was determined by X-ray diffraction at 2.8 A resolution. AnaB is a homotetramer and its fold is very similar to that of the acyl-CoA dehydrogenases (ACADs). The active-site base of AnaB, Glu244, superimposed very well with that of human isovaleryl-CoA dehydrogenase, confirming previous site-directed mutagenesis experiments and mechanistic proposals. The substrate-binding site of AnaB is small and is likely to be fitted for the pyrrolidine ring of proline. However, in contrast to ACADs, which use an electron-transport protein, AnaB uses molecular oxygen as the electron acceptor, as in acyl-CoA oxidases. Calculation of the solvent-accessible surface area around the FAD in AnaB and in several homologues showed that it is significantly larger in AnaB than in its homologues. A protonated histidine near the FAD in AnaB is likely to participate in oxygen activation. Furthermore, an array of water molecules detected in the AnaB structure suggests a possible path for molecular oxygen towards FAD. This is consistent with AnaB being an oxidase rather than a dehydrogenase. The structure of AnaB is the first to be described for a prolyl-ACP oxidase and it will contribute to defining the structural basis responsible for oxygen reactivity in flavoenzymes.

Structure of the prolyl-acyl carrier protein oxidase involved in the biosynthesis of the cyanotoxin anatoxin-a.,Moncoq K, Regad L, Mann S, Mejean A, Ploux O Acta Crystallogr D Biol Crystallogr. 2013 Dec;69(Pt 12):2340-52. doi:, 10.1107/S0907444913021859. Epub 2013 Nov 19. PMID:24311576<ref>PMID:24311576</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4irn" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Kamptonema sp. PCC 6506]]
[[Category: Large Structures]]
[[Category: Mann S]]
[[Category: Mejean A]]
[[Category: Moncoq K]]
[[Category: Ploux O]]
[[Category: Regad L]]