4nji | pdb_00004nji

Crystal Structure of QueE from Burkholderia multivorans in complex with AdoMet, 6-carboxy-5,6,7,8-tetrahydropterin, and Mg2+

spinqualitylabelsall models 4nji, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4nji is a 2 chain structure with sequence from Burkholderia multivorans ATCC 17616. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.197Å Ligands: 2K8, MG, NA, PO4, SAM Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function QUEE_BURM1 Catalyzes the complex heterocyclic radical-mediated conversion of 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) to 7-carboxy-7-deazaguanine (CDG), a step common to the biosynthetic pathways of all 7-deazapurine-containing compounds.[HAMAP-Rule:MF_00917] Publication Abstract from PubMed 7-carboxy-7-deazaguanine synthase (QueE) catalyzes a key S-adenosyl-L-methionine (AdoMet)- and Mg(2+)-dependent radical-mediated ring contraction step, which is common to the biosynthetic pathways of all deazapurine-containing compounds. QueE is a member of the AdoMet radical superfamily, which employs the 5'-deoxyadenosyl radical from reductive cleavage of AdoMet to initiate chemistry. To provide a mechanistic rationale for this elaborate transformation, we present the crystal structure of a QueE along with structures of pre- and post-turnover states. We find that substrate binds perpendicular to the [4Fe-4S]-bound AdoMet, exposing its C6 hydrogen atom for abstraction and generating the binding site for Mg(2+), which coordinates directly to the substrate. The Burkholderia multivorans structure reported here varies from all other previously characterized members of the AdoMet radical superfamily in that it contains a hypermodified (beta6/alpha3) protein core and an expanded cluster-binding motif, CX14CX2C. Radical SAM enzyme QueE defines a new minimal core fold and metal-dependent mechanism.,Dowling DP, Bruender NA, Young AP, McCarty RM, Bandarian V, Drennan CL Nat Chem Biol. 2014 Feb;10(2):106-12. doi: 10.1038/nchembio.1426. Epub 2013 Dec, 22. PMID:24362703 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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