Crystal structure of the effector binding domain of a CatM variant, CatM(V158M)Crystal structure of the effector binding domain of a CatM variant, CatM(V158M)
Structural highlights
2h98 is a 2 chain structure with sequence from Acinetobacter baylyi ADP1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
CATM_ACIAD Positively regulates the expression of catA, catBCIJFD and benPK in response to cis,cis-muconate. It binds to the catB-catM intercistronic region, to a specific sequence upstream of catA and to the benPK promoter region. Can also repress pca genes.[1][2][3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
↑Romero-Arroyo CE, Schell MA, Gaines GL 3rd, Neidle EL. catM encodes a LysR-type transcriptional activator regulating catechol degradation in Acinetobacter calcoaceticus. J Bacteriol. 1995 Oct;177(20):5891-8. PMID:7592340
↑Clark TJ, Momany C, Neidle EL. The benPK operon, proposed to play a role in transport, is part of a regulon for benzoate catabolism in Acinetobacter sp. strain ADP1. Microbiology. 2002 Apr;148(Pt 4):1213-23. PMID:11932465
↑Brzostowicz PC, Reams AB, Clark TJ, Neidle EL. Transcriptional cross-regulation of the catechol and protocatechuate branches of the beta-ketoadipate pathway contributes to carbon source-dependent expression of the Acinetobacter sp. strain ADP1 pobA gene. Appl Environ Microbiol. 2003 Mar;69(3):1598-606. PMID:12620848
