5g5g

Escherichia coli Periplasmic Aldehyde Oxidase

spinqualitylabelsall models 5g5g, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5g5g is a 3 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACT, CL, FAD, FES, GOL, IOD, MCN, MOS, SF4 NonStd Res: CSD Related: 5g5h Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [YAGT_ECOLI] Iron-sulfur subunit of the xanthine dehydrogenase complex. Publication Abstract from PubMed The xanthine oxidase (XO) family comprises molybdenum-dependent enzymes that usually form homodimers (or dimers of heterodimers/trimers) organized in three domains that harbor two [2Fe-2S] clusters, one FAD, and a Mo cofactor. In this work, we crystallized an unusual member of the family, the periplasmic aldehyde oxidoreductase PaoABC from Escherichia coli. This is the first example of an E. coli protein containing a molybdopterin-cytosine-dinucleotide cofactor and is the only heterotrimer of the XO family so far structurally characterized. The crystal structure revealed the presence of an unexpected [4Fe-4S] cluster, anchored to an additional 40 residues subdomain. According to phylogenetic analysis, proteins containing this cluster are widely spread in many bacteria phyla, putatively through repeated gene transfer events. The active site of PaoABC is highly exposed to the surface with no aromatic residues and an arginine (PaoC-R440) making a direct interaction with PaoC-E692, which acts as a base catalyst. In order to understand the importance of R440, kinetic assays were carried out, and the crystal structure of the PaoC-R440H variant was also determined. The Escherichia coli Periplasmic Aldehyde Oxidoreductase Is an Exceptional Member of the Xanthine Oxidase Family of Molybdoenzymes.,Correia MA, Otrelo-Cardoso AR, Schwuchow V, Sigfridsson Clauss KG, Haumann M, Romao MJ, Leimkuhler S, Santos-Silva T ACS Chem Biol. 2016 Sep 13. PMID:27622978 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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