4grs

Crystal structure of a chimeric DAH7PS

spinqualitylabelsall models 4grs, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4grs is a 4 chain structure with sequence from Pyrfu. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: TYR Related: 3pg9, 1zco Activity: 3-deoxy-7-phosphoheptulonate synthase, with EC number 2.5.1.54 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [AROF_THEMA] Catalyzes the condensation of phosphoenolpyruvate (PEP) and D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP). Publication Abstract from PubMed Allosteric regulation of protein function is a critical component of metabolic control. Its importance is underpinned by the diversity of mechanisms and its presence in all three domains of life. The first enzyme of the aromatic amino acid biosynthesis, 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase, shows remarkable variation in allosteric response and machinery, and both contemporary regulated and unregulated orthologs have been described. To examine the molecular events by which allostery can evolve, we have generated a chimeric protein by joining the catalytic domain of an unregulated 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase with the regulatory domain of a regulated enzyme. We demonstrate that this simple gene fusion event on its own is sufficient to confer functional allostery to the unregulated enzyme. The fusion protein shares structural similarities with its regulated parent protein and undergoes an analogous major conformational change in response to the binding of allosteric effector tyrosine to the regulatory domain. These findings help delineate a remarkably facile mechanism for the evolution of modular allostery by domain recruitment. Engineering allosteric control to an unregulated enzyme by transfer of a regulatory domain.,Cross PJ, Allison TM, Dobson RC, Jameson GB, Parker EJ Proc Natl Acad Sci U S A. 2013 Jan 23. PMID:23345433 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA