5ktl

Dihydrodipicolinate synthase from the industrial and evolutionarily important cyanobacteria Anabaena variabilis.

spinqualitylabelsall models 5ktl, resolution 1.92Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5ktl is a 2 chain structure with sequence from Anabaena atcc29413. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: MN NonStd Res: KPI Related: 5kt0 Gene: dapA, Ava_3607 (Anabaena ATCC29413) Activity: 4-hydroxy-tetrahydrodipicolinate synthase, with EC number 4.3.3.7 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [Q3M723_ANAVT] Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).[HAMAP-Rule:MF_00418][SAAS:SAAS00570606] Publication Abstract from PubMed Lysine biosynthesis in bacteria and plants commences with a condensation reaction catalysed by dihydrodipicolinate synthase (DHDPS) followed by a reduction reaction catalysed by dihydrodipicolinate reductase (DHDPR). Interestingly, both DHDPS and DHDPR exist as different oligomeric forms in bacteria and plants. DHDPS is primarily a homotetramer in all species, but the architecture of the tetramer differs across kingdoms. DHDPR also exists as a tetramer in bacteria, but has recently been reported to be dimeric in plants. This study aimed to characterise for the first time the structure and function of DHDPS and DHDPR from cyanobacteria, which is an evolutionary important phylum that evolved at the divergence point between bacteria and plants. We cloned, expressed and purified DHDPS and DHDPR from the cyanobacterium Anabaena variabilis. The recombinant enzymes were shown to be folded by circular dichroism spectroscopy, enzymatically active employing the quantitative DHDPS-DHDPR coupled assay, and form tetramers in solution using analytical ultracentrifugation. Crystal structures of DHDPS and DHDPR from A. variabilis were determined at 1.92 A and 2.83 A, respectively, and show that both enzymes adopt the canonical bacterial tetrameric architecture. These studies indicate that the quaternary structure of bacterial and plant DHDPS and DHDPR diverged after cyanobacteria evolved. Structure and Function of Cyanobacterial DHDPS and DHDPR.,Christensen JB, Soares da Costa TP, Faou P, Pearce FG, Panjikar S, Perugini MA Sci Rep. 2016 Nov 15;6:37111. doi: 10.1038/srep37111. PMID:27845445 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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