5c2x | pdb_00005c2x

Crystal structure of deoxyribose-phosphate aldolase from Colwellia psychrerythraea (tetragonal form)

spinqualitylabelsall models 5c2x, resolution 2.11Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5c2x is a 2 chain structure with sequence from "vibrio_psychroerythrus"_d'aoust_and_kushner_1972 "vibrio psychroerythrus" d'aoust and kushner 1972. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CO3, SO4, UNL Gene: deoC, CPS_1972 ("Vibrio psychroerythrus" D'Aoust and Kushner 1972) Activity: Deoxyribose-phosphate aldolase, with EC number 4.1.2.4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Understanding enzyme stability and activity in extremophilic organisms is of great biotechnological interest, but many questions are still unsolved. Using 2-deoxy-D-ribose-5-phosphate aldolase (DERA) as model enzyme, we have evaluated structural and functional characteristics of different orthologs from psychrophilic, mesophilic and hyperthermophilic organisms. We present the first crystal structures of psychrophilic DERAs, revealing a dimeric organization resembling their mesophilic but not their thermophilic counterparts. Conversion into monomeric proteins showed that the native dimer interface contributes to stability only in the hyperthermophilic enzymes. Nevertheless, introduction of a disulfide bridge in the interface of a psychrophilic DERA did confer increased thermostability, suggesting a strategy for rational design of more durable enzyme variants. Constraint network analysis revealed particularly sparse interactions between the substrate pocket and its surrounding alpha-helices in psychrophilic DERAs, which indicates that a more flexible active center underlies their high turnover numbers. Trading off stability against activity in extremophilic aldolases.,Dick M, Weiergraber OH, Classen T, Bisterfeld C, Bramski J, Gohlke H, Pietruszka J Sci Rep. 2016 Jan 19;6:17908. doi: 10.1038/srep17908. PMID:26783049 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Aldolase 3D structures

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