4aay

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (11:23, 20 December 2023) (edit) (undo)
 
(5 intermediate revisions not shown.)
Line 1: Line 1:
-
{{STRUCTURE_4aay| PDB=4aay | SCENE= }}
 
-
===Crystal Structure of the arsenite oxidase protein complex from Rhizobium species strain NT-26===
 
-
{{ABSTRACT_PUBMED_24023621}}
 
-
==About this Structure==
+
==Crystal Structure of the arsenite oxidase protein complex from Rhizobium species strain NT-26==
-
[[4aay]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Arsenite-oxidising_bacterium_nt-26 Arsenite-oxidising bacterium nt-26]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AAY OCA].
+
<StructureSection load='4aay' size='340' side='right'caption='[[4aay]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[4aay]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudorhizobium_banfieldiae Pseudorhizobium banfieldiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AAY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AAY 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]] 2.7&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4MO:MOLYBDENUM(IV)+ION'>4MO</scene>, <scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=MGD:2-AMINO-5,6-DIMERCAPTO-7-METHYL-3,7,8A,9-TETRAHYDRO-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-4-ONE+GUANOSINE+DINUCLEOTIDE'>MGD</scene>, <scene name='pdbligand=O:OXYGEN+ATOM'>O</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=4aay FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4aay OCA], [https://pdbe.org/4aay PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4aay RCSB], [https://www.ebi.ac.uk/pdbsum/4aay PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4aay ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/Q6VAL8_9HYPH Q6VAL8_9HYPH]
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The arsenite oxidase (Aio) from the facultative autotrophic Alphaproteobacterium Rhizobium sp. NT-26 is a bioenergetic enzyme involved in the oxidation of arsenite to arsenate. The enzyme from the distantly related heterotroph, Alcaligenes faecalis, which is thought to oxidise arsenite for detoxification, consists of a large alpha subunit (AioA) with bis-molybdopterin guanine dinucleotide at its active site and a 3Fe-4S cluster, and a small beta subunit (AioB) which contains a Rieske 2Fe-2S cluster. The successful heterologous expression of the NT-26 Aio in Escherichia coli has resulted in the solution of its crystal structure. The NT-26 Aio, a heterotetramer, shares high overall similarity to the heterodimeric arsenite oxidase from A. faecalis but there are striking differences in the structure surrounding the Rieske 2Fe-2S cluster which we demonstrate explains the difference in the observed redox potentials (+225 mV vs. +130/160 mV, respectively). A combination of site-directed mutagenesis and electron paramagnetic resonance was used to explore the differences observed in the structure and redox properties of the Rieske cluster. In the NT-26 AioB the substitution of a serine (S126 in NT-26) for a threonine as in the A. faecalis AioB explains a -20 mV decrease in redox potential. The disulphide bridge in the A. faecalis AioB which is conserved in other betaproteobacterial AioB subunits and the Rieske subunit of the cytochrome bc 1 complex is absent in the NT-26 AioB subunit. The introduction of a disulphide bridge had no effect on Aio activity or protein stability but resulted in a decrease in the redox potential of the cluster. These results are in conflict with previous data on the betaproteobacterial AioB subunit and the Rieske of the bc 1 complex where removal of the disulphide bridge had no effect on the redox potential of the former but a decrease in cluster stability was observed in the latter.
-
==Reference==
+
The respiratory arsenite oxidase: structure and the role of residues surrounding the rieske cluster.,Warelow TP, Oke M, Schoepp-Cothenet B, Dahl JU, Bruselat N, Sivalingam GN, Leimkuhler S, Thalassinos K, Kappler U, Naismith JH, Santini JM PLoS One. 2013 Aug 30;8(8):e72535. doi: 10.1371/journal.pone.0072535. PMID:24023621<ref>PMID:24023621</ref>
-
<ref group="xtra">PMID:024023621</ref><references group="xtra"/><references/>
+
 
-
[[Category: Arsenite-oxidising bacterium nt-26]]
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
[[Category: Naismith, J H.]]
+
</div>
-
[[Category: Oke, M.]]
+
<div class="pdbe-citations 4aay" style="background-color:#fffaf0;"></div>
-
[[Category: Santini, J M.]]
+
== References ==
-
[[Category: Iron sulfur]]
+
<references/>
-
[[Category: Molybdopterin]]
+
__TOC__
-
[[Category: Oxidoreductase]]
+
</StructureSection>
-
[[Category: Rieske]]
+
[[Category: Large Structures]]
 +
[[Category: Pseudorhizobium banfieldiae]]
 +
[[Category: Naismith JH]]
 +
[[Category: Oke M]]
 +
[[Category: Santini JM]]

Current revision

Crystal Structure of the arsenite oxidase protein complex from Rhizobium species strain NT-26

PDB ID 4aay

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4aay"
Personal tools