6gnf
Granule Bound Starch Synthase from Cyanobacterium sp. CLg1 bound to acarbose and ADPGranule Bound Starch Synthase from Cyanobacterium sp. CLg1 bound to acarbose and ADP
Structural highlights
Function[V5SNJ5_9CHRO] Synthesizes alpha-1,4-glucan chains using ADP-glucose.[HAMAP-Rule:MF_00484][SAAS:SAAS00746778] Publication Abstract from PubMedStarch synthases (SSs) are responsible for depositing the majority of glucoses in starch. Structural knowledge on these enzymes that is available from the crystal structures of rice granule bound starch synthase (GBSS) and barley SSI provides incomplete information on substrate binding and active site architecture. Here we report the crystal structures of the catalytic domains of SSIV from Arabidopsis thaliana, of GBSS from the cyanobacterium CLg1 and GBSSI from the glaucophyte Cyanophora paradoxa, with all three bound to ADP and the inhibitor acarbose. The SSIV structure illustrates in detail the modes of binding for both donor and acceptor in a plant SS. CLg1GBSS contains, in the same crystal structure, examples of molecules with and without bound acceptor, which illustrates the conformational changes induced upon acceptor binding that presumably precede catalytic activity. With structures available from several isoforms of plant and non-plant SSs, as well as the closely related bacterial glycogen synthases, we analyze, at the structural level, the common elements that define a SS, the elements that are necessary for substrate binding and singularities of the GBSS family that could underlie its processivity. While the phylogeny of the SSIII/IV/V has been recently discussed, we now further report the detailed evolutionary history of the GBSS/SSI/SSII type of SSs enlightening the origin of the GBSS enzymes used in our structural analysis. Crystal Structures of the Catalytic Domain of Arabidopsis thaliana Starch Synthase IV, of Granule Bound Starch Synthase From CLg1 and of Granule Bound Starch Synthase I of Cyanophora paradoxa Illustrate Substrate Recognition in Starch Synthases.,Nielsen MM, Ruzanski C, Krucewicz K, Striebeck A, Cenci U, Ball SG, Palcic MM, Cuesta-Seijo JA Front Plant Sci. 2018 Aug 3;9:1138. doi: 10.3389/fpls.2018.01138. eCollection, 2018. PMID:30123236[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||||