putA Antibody

1. Deletion of the C-terminal motif (CCM) or replacement of hydrophobic residues with negatively charged residues within the CCM impairs EcPutA functional and physical membrane association PMID: 29090935
2. crystal structures of the proline dehydrogenase domain mutants PutA86-630D370N and PutA86-630D370A complexed with the proline analogue show that the mutations cause only minor perturbations to the active site but no major structural changes PMID: 23713611
3. Data show that PutA is a symmetric V-shaped dimer having dimensions of 205 x 85 x 55 A. The particle consists of two large lobes connected by a 30-A diameter cylinder PMID: 22013066
4. kinetic data, along with analysis of crystal structure data for the PRODH domain, suggest that the proline:ubiquinone oxidoreductase reaction occurs via a rapid equilibrium ping-pong mechanism with proline and ubiquinone binding at two distinct sites PMID: 22040654
5. The proline dehydrogenase (PRODH)/L-tetrahydro-2-furoic acid complex is the first structure of PRODH with a five-membered ring proline analogue bound in the active site. PMID: 15449943
6. From this study it is clear that reduction of flavin adenine dinucleotide bound to the proline dehydrogenase active site of PutA elicits global conforamtional changes that direct PutA-membrane associations. PMID: 15476410
7. identify molecular interactions in the PutA active site that underlie redox-dependent functional switching of PutA PMID: 17209558
8. analysis of metabolism and gene expression in the proline utilization A protein from Escherichia coli [review] PMID: 18324349

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KEGG: ecj:JW0999

STRING: 316385.ECDH10B_1086