1r23 | pdb_00001r23

Crystal structure of the cyanobacterial metallothionein repressor SmtB in the Zn1-form (one Zn(II) per dimer)

spinqualitylabelsall models 1r23, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1r23 is a 2 chain structure with sequence from Anacystis nidulans r2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ZN Related: 1r1t, 1smt, 1r22, 1r1u, 1r1v Gene: SMTB (Anacystis nidulans R2) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [SMTB_SYNE7] Transcriptional repressor of the expression of the smtA gene. Binds two zinc ions per dimer. The complex of DNA and SmtB is dissociated by zinc ions. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The origin of metal ion selectivity by members of the SmtB/ArsR family of bacterial metal-sensing transcriptional repressors and the mechanism of negative allosteric regulation of DNA binding is poorly understood. Here, we report that two homologous zinc sensors, Staphylococcus aureus CzrA and cyanobacterial SmtB, are "winged" helix homodimeric DNA-binding proteins that bind Zn(II) to a pair of tetrahedral, interhelical binding sites, with two ligands derived from the alpha5 helix of one subunit, Asp84 O(delta1) (Asp104 in SmtB), His86 N(delta1) (His106), and two derived from the alpha5 helix of the other, His97' N(delta1) (His117') and His100' N(epsilon2) (Glu120'). Formation of the metal chelate drives a quaternary structural switch mediated by an intersubunit hydrogen-binding network that originates with the non-liganding N(epsilon2) face of His97 in CzrA (His117 in SmtB) that stabilizes a low-affinity, DNA-binding conformation. The structure of the Zn(1) SmtB homodimer shows that both metal-binding sites of the dimer must be occupied for the quaternary structural switch to occur. Thus, a critical zinc-ligating histidine residue obligatorily couples formation of the metal-sensing coordination chelate to changes in the conformation and dynamics of the putative DNA-binding helices. A metal-ligand-mediated intersubunit allosteric switch in related SmtB/ArsR zinc sensor proteins.,Eicken C, Pennella MA, Chen X, Koshlap KM, VanZile ML, Sacchettini JC, Giedroc DP J Mol Biol. 2003 Oct 31;333(4):683-95. PMID:14568530 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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