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Table 2 Characteristic features of NAGK (3D-crystal structure) from various organisms

From: Insight into de-regulation of amino acid feedback inhibition: a focus on structure analysis method

Enzyme

Structural composition

Key structural features

3D-view of structure (cartoon representation)

Reference

NAGK (Yeast)

Tetramer

Central structure is a flat tetramer formed by two dimers of AAK domains

Bound arginine and NAG

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[91]

NAGK (E.coli)

Homodimer

Each subunit comprised of two lobes (i.e. C-lobe binds ADP moiety of ATP and N-lobe forms inter subunit surface

Arginine free

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[47, 92]

NAGK (T. maritima)

Hexamer

Formed by linking three E. coli NAGK-like homodimers through the interlacing of an N-terminal mobile kinked a-helix

Arginine is bound in each subunit flanking the interdimeric junction, in a site formed between the N helix and the C lobe of the subunit

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[47]

NAGK (P. aurogenosa)

Hexamer (Ring-like)

Arginine free

Bound NAG and ADP-Mg

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[47, 91]

NAGK (C. crenatum

Swiss model hexamer (Ring-like)

Arginine binding domain comprised of Glu19, His26, Arg209 and His268

Glu19 at entrance of binding site is key amino acid

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[93]