LeuA_dimer

LeuA allosteric (dimerisation) domain
LeuA_dimer
SMART accession number:SM00917
Description: This is the C-terminal regulatory (R) domain of alpha-isopropylmalate synthase, which catalyses the first committed step in the leucine biosynthetic pathway (PUBMED:15159544). This domain, is an internally duplicated structure with a novel fold (PUBMED:15159544). It comprises two similar units that are arranged such that the two -helices pack together in the centre, crossing at an angle of 34 degrees, sandwiched between the two three-stranded, antiparallel beta-sheets. The overall domain is thus constructed as a beta-alpha-beta three-layer sandwich (PUBMED:15159544).
Interpro abstract (IPR013709):

This is the C-terminal regulatory (R) domain of alpha-isopropylmalate synthase, which catalyses the first committed step in the leucine biosynthetic pathway [(PUBMED:15159544)]. This domain, is an internally duplicated structure with a novel fold [(PUBMED:15159544)]. It comprises two similar units that are arranged such that the two -helices pack together in the centre, crossing at an angle of 34 degrees, sandwiched between the two three-stranded, antiparallel beta-sheets. The overall domain is thus constructed as a beta-alpha-beta three-layer sandwich [(PUBMED:15159544)].

GO process:leucine biosynthetic process (GO:0009098)
GO function:2-isopropylmalate synthase activity (GO:0003852)
Family alignment:
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There are 2072 LeuA_dimer domains in 2071 proteins in SMART's nrdb database.

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