5C5Y: Crystal Structure Of Deoxyribose-phosphate Aldolase From Colwellia Psychrerythraea (hexagonal Form)

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.
PDB ID: 5C5YDownload
MMDB ID: 136199
PDB Deposition Date: 2015/6/22
Updated in MMDB: 2016/02
Experimental Method:
x-ray diffraction
Resolution: 2.1  Å
Source Organism:
Similar Structures:
Biological Unit for 5C5Y: dimeric; determined by author
Molecular Components in 5C5Y
Label Count Molecule
Proteins (2 molecules)
Deoxyribose-phosphate Aldolase
Molecule annotation
Chemicals (5 molecules)
* Click molecule labels to explore molecular sequence information.

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