4aty | pdb_00004aty

Crystal structure of a Terephthalate 1,2-cis-dihydrodioldehydrogenase from Burkholderia xenovorans LB400

spinqualitylabelsall models 4aty, resolution 1.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4aty is a 1 chain structure with sequence from Burkholderia cepacia lb400. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BME, ZN Activity: 4-hydroxythreonine-4-phosphate dehydrogenase, with EC number 1.1.1.262 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed As a highly coveted precursor molecule, terephthalate (Tph) continues to be used extensively for the production of polyethylene Tph bottles, polyester films, and textile fibers worldwide. Based on its detrimental physiological effects, Tph is now recognized as a serious environmental pollutant. While amenable to biodegradation and, in fact, traditionally neutralized by aerobic microbiological processes, our current lack of understanding of the enzymatic degradation of Tph at the molecular level presents a major impediment in the development of robust bioremediation strategies. The biodegradation of Tph proceeds through a single metabolic intermediate (a cis-dihydrodiol), which is subsequently converted to the end product (protocatechuate) by a decarboxylating cis-dihydrodiol dehydrogenase (TphB). Using iodide single-wavelength anomalous dispersion, we report the first structural characterization of TphB to 1.85A resolution. Contrary to prior speculations, a fluorescent scan unambiguously shows that TphB coordinates Zn(2+) and not Fe(2+). The molecular architecture of TphB provides a rationale to the primary-level divergence observed between TphB and other cis-dihydrodiol dehydrogenases while explaining its intriguingly close evolutionary clustering with non-dihydrodiol dehydrogenases belonging to the isocitrate/isopropylmalate family of enzymes. Sequence and structural analyses reveal a putative substrate-binding pocket proximal to the bound Zn(2+). In silico substrate modeling in this putative binding pocket suggests a mechanistic sequence relying on H291, K295, and Zn(2+) as core mediators of catalytic turnover. Overall, this study reveals novel structural and mechanistic insights into a decarboxylating cis-dihydrodiol dehydrogenase that mediates one of the two catalytic steps in the biodegradation of the environmental pollutant Tph. Investigating Terephthalate Biodegradation: Structural Characterization of a Putative Decarboxylating cis-Dihydrodiol Dehydrogenase.,Bains J, Wulff JE, Boulanger MJ J Mol Biol. 2012 Oct 26;423(3):284-93. doi: 10.1016/j.jmb.2012.07.022. Epub 2012 , Aug 11. PMID:22889862 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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