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2VI7

Structure of a Putative Acetyltransferase (PA1377)from Pseudomonas aeruginosa

Summary for 2VI7
Entry DOI10.2210/pdb2vi7/pdb
DescriptorACETYLTRANSFERASE PA1377, GLYCEROL, SULFATE ION, ... (5 entities in total)
Functional Keywordsgnat, gcn5 family, transferase, n-acetyltransferase, hypothetical protein
Biological sourcePSEUDOMONAS AERUGINOSA
Total number of polymer chains3
Total formula weight61498.25
Authors
Davies, A.M.,Tata, R.,Chauviac, F.X.,Sutton, B.J.,Brown, P.R. (deposition date: 2007-11-28, release date: 2008-05-20, Last modification date: 2023-12-13)
Primary citationDavies, A.M.,Tata, R.,Chauviac, F.X.,Sutton, B.J.,Brown, P.R.
Structure of a Putative Acetyltransferase (Pa1377) from Pseudomonas Aeruginosa.
Acta Crystallogr.,Sect.F, 64:338-, 2008
Cited by
PubMed Abstract: 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 I222 to 2.25 A resolution. Pitax belongs to the GCN5-related N-acetyltransferase family and contains all four sequence motifs conserved among family members. The beta-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.
PubMed: 18453699
DOI: 10.1107/S1744309108007665
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.25 Å)
Structure validation

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