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Structure of a putative acetyltransferase (PA1377) from Pseudomonas aeruginosa
Author(s) -
Davies Anna M.,
Tata Renée,
Chauviac FrançoisXavier,
Sutton Brian J.,
Brown Paul R.
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108007665
Subject(s) - pseudomonas aeruginosa , acetyltransferase , microbiology and biotechnology , chemistry , biology , genetics , biochemistry , bacteria , gene , acetylation
Gene PA1377 from Pseudomonas aeruginosa encodes a 177‐amino‐acid conserved hypothetical protein of unknown function. The structure of this protein (termed pitax) has been solved in space group I 222 to 2.25 Å resolution. Pitax belongs to the GCN5‐related N ‐acetyltransferase family and contains all four sequence motifs conserved among family members. The β‐strand structure in one of these motifs (motif A ) is disrupted, which is believed to affect binding of the substrate that accepts the acetyl group from acetyl‐CoA.

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