Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.7.8.43 extracted from

  • Stogios, P.J.; Cox, G.; Zubyk, H.L.; Evdokimova, E.; Wawrzak, Z.; Wright, G.D.; Savchenko, A.
    Substrate recognition by a colistin resistance enzyme from Moraxella catarrhalis (2018), ACS Chem. Biol., 13, 1322-1332 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.8.43

Crystallization (Commentary)

Crystallization (Comment) Organism
structure of the catalytic domain of ICR.. Catalytic domain dimerization is required for substrate binding. The structure reveals two disulfide bonds (Cys390 to Cys398, Cys448 to Cys456) Moraxella sp. HMSC061H09

Protein Variants

Protein Variants Comment Organism
T315A mutation of the catalytic domain, abolishes antibiotic resistance activity Moraxella sp. HMSC061H09

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ a single Zn2+ atom is bound to ICR active site Moraxella sp. HMSC061H09

Organism

Organism UniProt Comment Textmining
Moraxella sp. HMSC061H09 A0A1E9VP98
-
-

Synonyms

Synonyms Comment Organism
colistin resistance PEtN transferase
-
 Moraxella sp. HMSC061H09
HMPREF2573_04170
-
 Moraxella sp. HMSC061H09
ICR
-
 Moraxella sp. HMSC061H09
intrinsic colistin resistance enzyme
-
 Moraxella sp. HMSC061H09

General Information

General Information Comment Organism
physiological function expression in Escherichia coli leads to 4fold increase in resistance to antibiotics colistin and polymyxin B. In addition to the catalytoc domain, the N-terminal transmembrane regions are required to confer drug resistance in the cell Moraxella sp. HMSC061H09