5G5G
Escherichia coli Periplasmic Aldehyde Oxidase
Summary for 5G5G
| Entry DOI | 10.2210/pdb5g5g/pdb |
| Related | 5G5H |
| Descriptor | PUTATIVE XANTHINE DEHYDROGENASE YAGT IRON-SULFUR-BINDING SUBUNIT, FLAVIN-ADENINE DINUCLEOTIDE, PTERIN CYTOSINE DINUCLEOTIDE, ... (13 entities in total) |
| Functional Keywords | oxidoreductase, paoabc, xanthine oxidase family, heterotrimer, e.coli detoxification |
| Biological source | ESCHERICHIA COLI More |
| Total number of polymer chains | 3 |
| Total formula weight | 140900.61 |
| Authors | Correia, M.A.S.,Otrelo-Cardoso, A.R.,Romao, M.J.,Santos-Silva, T. (deposition date: 2016-05-25, release date: 2016-09-28, Last modification date: 2024-01-10) |
| Primary citation | Correia, M.A.,Otrelo-Cardoso, A.R.,Schwuchow, V.,Sigfridsson Clauss, K.G.,Haumann, M.,Romao, M.J.,Leimkuhler, S.,Santos-Silva, T. The Escherichia Coli Periplasmic Aldehyde Oxidoreductase is an Exceptional Member of the Xanthine Oxidase Family of Molybdoenzymes. Acs Chem.Biol., 11:2923-, 2016 Cited by PubMed Abstract: 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. PubMed: 27622978DOI: 10.1021/ACSCHEMBIO.6B00572 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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