2H99
Crystal structure of the effector binding domain of a BenM variant (R156H,T157S)
Summary for 2H99
| Entry DOI | 10.2210/pdb2h99/pdb |
| Related | 2F6P 2F78 2F7A 2F7B 2F8D 2F97 2H98 2H9B 2H9Q |
| Descriptor | HTH-type transcriptional regulator benM, SULFATE ION, ACETATE ION, ... (6 entities in total) |
| Functional Keywords | lttr, benm, transcriptional regulation, catm, transcription |
| Biological source | Acinetobacter sp. |
| Total number of polymer chains | 2 |
| Total formula weight | 72127.00 |
| Authors | Ezezika, O.C.,Craven, S.H.,Neidle, E.L.,Momany, C. (deposition date: 2006-06-09, release date: 2007-06-26, Last modification date: 2023-08-30) |
| Primary citation | Craven, S.H.,Ezezika, O.C.,Haddad, S.,Hall, R.A.,Momany, C.,Neidle, E.L. Inducer responses of BenM, a LysR-type transcriptional regulator from Acinetobacter baylyi ADP1. Mol.Microbiol., 72:881-894, 2009 Cited by PubMed Abstract: BenM and CatM control transcription of a complex regulon for aromatic compound degradation. These Acinetobacter baylyi paralogues belong to the largest family of prokaryotic transcriptional regulators, the LysR-type proteins. Whereas BenM activates transcription synergistically in response to two effectors, benzoate and cis,cis-muconate, CatM responds only to cis,cis-muconate. Here, site-directed mutagenesis was used to determine the physiological significance of an unexpected benzoate-binding pocket in BenM discovered during structural studies. Residues in BenM were changed to match those of CatM in this hydrophobic pocket. Two BenM residues, R160 and Y293, were found to mediate the response to benzoate. Additionally, alteration of these residues caused benzoate to inhibit activation by cis,cis-muconate, positioned in a separate primary effector-binding site of BenM. The location of the primary site, in an interdomain cleft, is conserved in diverse LysR-type regulators. To improve understanding of this important family, additional regulatory mutants were analysed. The atomic-level structures were characterized of the effector-binding domains of variants that do not require inducers for activation, CatM(R156H) and BenM(R156H,T157S). These structures clearly resemble those of the wild-type proteins in their activated muconate-bound complexes. Amino acid replacements that enable activation without effectors reside at protein interfaces that may impact transcription through effects on oligomerization. PubMed: 19400783DOI: 10.1111/j.1365-2958.2009.06686.x PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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