Theme D Highlights

Theme D links with Warwick, siderophore biosynthesis. Last year we reported the structure of AcsD in the apo form. This year we have determined the structure of the AcsD with citrate (2.3 Å) and ATP (2.1Å). The ATP binding fold is indeed novel and the citrate complex rationalizes kinetic observation of the citrate substrate inhibition. The work is now being written for publication.
The structure of AlcC, a type C siderophore synthetase, with a molecular weight of 70,605 Da from Bordetellae, has been determined to 2.4 Å. Crystal symmetry generates a dimer. The fold of the protein is related to AcsD, although the homology is quite low preventing a molecular replacement solution. Mechanistically the adenyl transfer reaction will be related to AcsD, however substrate specificity is quite different. Additionally type C enzymes are often processive, the structure of AlcC will greatly help in our understanding siderophore biosynthesis. It also present a novel target for drug design.






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Updated:30-10-07