6hte | pdb_00006hte

Sulfolobus solfataricus Tryptophan Synthase B2a

spinqualitylabelsall models 6hte, resolution 1.96Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6hte is a 2 chain structure with sequence from Saccharolobus solfataricus. This structure supersedes the now removed PDB entry 6eqn. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.961Å Ligands: PEG, PLP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function TRPB2_SACS2 The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. Publication Abstract from PubMed Tryptophan synthase (TrpS) is a heterotetrameric alphabetabetaalpha enzyme that exhibits complex substrate channeling and allosteric mechanisms and is a model system in enzymology. In this work, we characterize proposed early and late evolutionary states of TrpS and show that they have distinct quaternary structures, caused by insertions-deletions of sequence segments (indels) in the beta-subunit. Remarkably, indole hydrophobic channels that connect alpha and beta active sites have re-emerged in both TrpS types, yet they follow different paths through the beta-subunit fold. Also, both TrpS geometries activate the alpha-subunit through the rearrangement of loops flanking the active site. Our results link evolutionary sequence changes in the enzyme subunits with channeling and allostery in the TrpS enzymes. The findings demonstrate that indels allow protein quaternary architectures to scape "minima" in the evolutionary landscape, thereby overcoming the conservational constraints imposed by existing functional interfaces and being free to morph into new mechanistic enzymes. Evolutionary Morphing of Tryptophan Synthase: Functional Mechanisms for the Enzymatic Channeling of Indole.,Fleming JR, Schupfner M, Busch F, Basle A, Ehrmann A, Sterner R, Mayans O J Mol Biol. 2018 Oct 24. pii: S0022-2836(18)30606-5. doi:, 10.1016/j.jmb.2018.10.013. PMID:30367843 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Tryptophan synthase 3D structures

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