4rg8

Structural and biochemical studies of a moderately thermophilic Exonuclease I from Methylocaldum szegediense

spinqualitylabelsall models 4rg8, resolution 2.12Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4rg8 is a 1 chain structure with sequence from Methylocaldum szegediense. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.12Å Ligands: MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0A0R5X6_9GAMM Publication Abstract from PubMed A novel exonuclease, designated as MszExo I, was cloned from Methylocaldum szegediense, a moderately thermophilic methanotroph. It specifically digests single-stranded DNA in the 3' to 5' direction. The protein is composed of 479 amino acids, and it shares 47% sequence identity with E. coli Exo I. The crystal structure of MszExo I was determined to a resolution of 2.2 A and it aligns well with that of E. coli Exo I. Comparative studies revealed that MszExo I and E. coli Exo I have similar metal ion binding affinity and similar activity at mesophilic temperatures (25-47 degrees C). However, the optimum working temperature of MszExo I is 10 degrees C higher, and the melting temperature is more than 4 degrees C higher as evaluated by both thermal inactivation assays and DSC measurements. More importantly, two thermal transitions during unfolding of MszExo I were monitored by DSC while only one transition was found in E. coli Exo I. Further analyses showed that magnesium ions not only confer structural stability, but also affect the unfolding of MszExo I. MszExo I is the first reported enzyme in the DNA repair systems of moderately thermophilic bacteria, which are predicted to have more efficient DNA repair systems than mesophilic ones. Structural and biochemical studies of a moderately thermophilic exonuclease I from Methylocaldum szegediense.,Fei L, Tian S, Moysey R, Misca M, Barker JJ, Smith MA, McEwan PA, Pilka ES, Crawley L, Evans T, Sun D PLoS One. 2015 Feb 6;10(2):e0117470. doi: 10.1371/journal.pone.0117470., eCollection 2015. PMID:25658953 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Exonuclease 3D structures

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