2f8d | pdb_00002f8d

BenM effector-Binding domain crystallized from high pH conditions

spinqualitylabelsall models 2f8d, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2f8d is a 2 chain structure with sequence from Acibi. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BEZ, GOL, PO4 Related: 2f6g, 2f6p, 2f78, 2f7a, 2f7b, 2f7c, 2f97 Gene: benM (ACIBI) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [BENM_ACIAD] Positive regulator of the ben and cat genes for benzoate degradation. BenM is necessary for ben gene expression but not for expression of the cat genes, which can be regulated by CatM. Binds to the inducers cis,cis-muconate and benzoate. 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 LysR-type transcriptional regulators comprise the largest family of homologous regulatory DNA-binding proteins in bacteria. A problematic challenge in the crystallization of LysR-type regulators stems from the insolubility and precipitation difficulties encountered with high concentrations of the full-length versions of these proteins. A general oligomerization scheme is proposed for this protein family based on the structures of the effector-binding domain of BenM in two different space groups, P4(3)22 and C222(1). These structures used the same oligomerization scheme of dimer-dimer interactions as another LysR-type regulator, CbnR, the full-length structure of which is available [Muraoka et al. (2003), J. Mol. Biol. 328, 555-566]. Evaluation of packing relationships and surface features suggests that BenM can form infinite oligomeric arrays in crystals through these dimer-dimer interactions. By extrapolation to the liquid phase, such dimer-dimer interactions may contribute to the significant difficulty in crystallizing full-length members of this family. The oligomerization of dimeric units to form biologically important tetramers appears to leave unsatisfied oligomerization sites. Under conditions that favor association, such as neutral pH and concentrations appropriate for crystallization, higher order oligomerization could cause solubility problems with purified proteins. A detailed model by which BenM and other LysR-type transcriptional regulators may form these arrays is proposed. Oligomerization of BenM, a LysR-type transcriptional regulator: structural basis for the aggregation of proteins in this family.,Ezezika OC, Haddad S, Neidle EL, Momany C Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 May 1;63(Pt, 5):361-8. Epub 2007 Apr 28. PMID:17565172 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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