4bs9
Structure of the heterocyclase TruDStructure of the heterocyclase TruD
Structural highlights
FunctionPublication Abstract from PubMedCounting backwards: The cyanobactin class of heterocyclases, exemplified by TruD, possess an almost unique combination of processivity, specificity, chemical versatility, and promiscuity. TruD is shown by biochemical assay to be an adenylase, and processes cysteines in a defined order. The entire substrate leader can be removed and TruD will process a single specific cysteine residue; however the role of leader is to permit processivity through a balance of recognition. ATP/AMP=adenosine tri/monophosphate; PPi=pyrophosphate. The Cyanobactin Heterocyclase Enzyme: A Processive Adenylase That Operates with a Defined Order of Reaction.,Koehnke J, Bent AF, Zollman D, Smith K, Houssen WE, Zhu X, Mann G, Lebl T, Scharff R, Shirran S, Botting CH, Jaspars M, Schwarz-Linek U, Naismith JH Angew Chem Int Ed Engl. 2013 Nov 8. doi: 10.1002/anie.201306302. PMID:24214017[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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