5ktt | pdb_00005ktt

Crystal structure of Pyrococcus horikoshii quinolinate synthase (NadA) with bound L-malate and Fe4S4 cluster

spinqualitylabelsall models 5ktt, resolution 1.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5ktt is a 1 chain structure with sequence from Pyrococcus horikoshii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: LMR, SF4 Related: 5kts, 5ktm, 5ktr, 5kto, 5ktn, 5ktp Gene: nadA, PH0013 (Pyrococcus horikoshii) Activity: Quinolinate synthase, with EC number 2.5.1.72 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [NADA_PYRHO] Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate (By similarity). Publication Abstract from PubMed The quinolinate synthase of prokaryotes and photosynthetic eukaryotes, NadA, contains a [4Fe-4S] cluster with unknown function. We report crystal structures of Pyrococcus horikoshii NadA in complex with dihydroxyacetone phosphate (DHAP), iminoaspartate analogues, and quinolinate. DHAP adopts a nearly planar conformation and chelates the [4Fe-4S] cluster via its keto and hydroxyl groups. The active site architecture suggests that the cluster acts as a Lewis acid in enediolate formation, like zinc in class II aldolases. The DHAP and putative iminoaspartate structures suggest a model for a condensed intermediate. The ensemble of structures suggests a two-state system, which may be exploited in early steps. Crystal Structures of the Iron-Sulfur Cluster-Dependent Quinolinate Synthase in Complex with Dihydroxyacetone Phosphate, Iminoaspartate Analogues, and Quinolinate.,Fenwick MK, Ealick SE Biochemistry. 2016 Jul 22. PMID:27404889 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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