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2Q5Z

Crystal structure of iMazG from Vibrio DAT 722: Ntag-iMazG (P43212)

Summary for 2Q5Z
Entry DOI10.2210/pdb2q5z/pdb
Related2Q73
DescriptorHypothetical protein, MAGNESIUM ION, GLYCEROL, ... (4 entities in total)
Functional Keywordsmazg, vibrio, ntp-ppase, hydrolase
Biological sourceVibrio sp. DAT722
Total number of polymer chains2
Total formula weight26424.30
Authors
Robinson, A.,Guilfoyle, A.P.,Harrop, S.J.,Boucher, Y.,Stokes, H.W.,Curmi, P.M.G.,Mabbutt, B.C. (deposition date: 2007-06-04, release date: 2007-10-09, Last modification date: 2023-08-30)
Primary citationRobinson, A.,Guilfoyle, A.P.,Harrop, S.J.,Boucher, Y.,Stokes, H.W.,Curmi, P.M.,Mabbutt, B.C.
A putative house-cleaning enzyme encoded within an integron array: 1.8 A crystal structure defines a new MazG subtype.
Mol.Microbiol., 66:610-621, 2007
Cited by
PubMed Abstract: Mobile gene cassettes collectively contain a highly diverse pool of novel genes that encode many novel adaptive functions. In the non-clinical context, the function of almost all of the encoded proteins remains unknown despite the enormous size of this mobile gene pool. We have been characterizing cassette arrays by taking advantage of the fact that they cluster at discrete sites in chromosomes; even large arrays are thus recoverable in a relatively small number of clones in genomic libraries. In one assembled array of 116 cassettes from the marine bacterium Vibrio sp. DAT722, a putative MazG protein is encoded within the 21st cassette. Because MazG proteins are implicated in a number of cellular processes, including house-cleaning and stress survival, the presence of such a protein in a mobile cassette was noteworthy. Here we solve the crystal structure of this alpha-helical protein, and define both open and closed states of a new variant of the MazG family. Functional assays confirm that the protein is a dNTP pyrophosphohydrolase, with marked preferences for dCTP and dATP. We hypothesize that iMazG acts as a house-cleaning enzyme, preventing the incorporation of damaging non-canonical nucleotides into host-cell DNA.
PubMed: 17892463
DOI: 10.1111/j.1365-2958.2007.05932.x
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.3 Å)
Structure validation

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数据于2024-10-30公开中

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