6y7a | pdb_00006y7a

X-ray structure of the Haloalkane dehalogenase HaloTag7 labeled with a chloroalkane-tetramethylrhodamine fluorophore substrate

spinqualitylabelsall models 6y7a, resolution 1.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6y7a is a 1 chain structure with sequence from Rhodococcus sp.. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.4Å Ligands: CL, GOL, OEH Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function DHAA_RHOSO Publication Abstract from PubMed The self-labeling protein tags (SLPs) HaloTag7, SNAP-tag, and CLIP-tag allow the covalent labeling of fusion proteins with synthetic molecules for applications in bioimaging and biotechnology. To guide the selection of an SLP-substrate pair and provide guidelines for the design of substrates, we report a systematic and comparative study of the labeling kinetics and substrate specificities of HaloTag7, SNAP-tag, and CLIP-tag. HaloTag7 reaches almost diffusion-limited labeling rate constants with certain rhodamine substrates, which are more than 2 orders of magnitude higher than those of SNAP-tag for the corresponding substrates. SNAP-tag labeling rate constants, however, are less affected by the structure of the label than those of HaloTag7, which vary over 6 orders of magnitude for commonly employed substrates. Determining the crystal structures of HaloTag7 and SNAP-tag labeled with fluorescent substrates allowed us to rationalize their substrate preferences. We also demonstrate how these insights can be exploited to design substrates with improved labeling kinetics. Kinetic and Structural Characterization of the Self-Labeling Protein Tags HaloTag7, SNAP-tag, and CLIP-tag.,Wilhelm J, Kuhn S, Tarnawski M, Gotthard G, Tunnermann J, Tanzer T, Karpenko J, Mertes N, Xue L, Uhrig U, Reinstein J, Hiblot J, Johnsson K Biochemistry. 2021 Aug 24;60(33):2560-2575. doi: 10.1021/acs.biochem.1c00258., Epub 2021 Aug 2. PMID:34339177 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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