1BO4: Crystal Structure Of A Gcn5-Related N-Acetyltransferase: Serratia Marescens Aminoglycoside 3-N-Acetyltransferase

The X-ray structure of a canonical GCN5-related N-acetyltransferase (GNAT), Serratia marcescens aminoglycoside 3-N-acetyltransferase, bound to coenzyme A (CoA) has been determined at 2.3 A resolution. The single domain alpha/beta protein resembles a cupped right hand wrapped around a cylinder and consists of a highly curved, six-stranded beta sheet of mixed polarity that is sandwiched between four alpha helices. The structure includes all four conserved GNAT motifs (C, D, A, and B) and represents the catalytic core of this large enzyme superfamily. Acetyl CoA recognition is mediated by a betaalpha structure derived from GNAT motif A, which presents an invariant Arg/Gln-X-X-Gly-X-Gly/Ala segment for hydrogen bonding with the cofactor. Motif B contributes acidic residues to the binding site for the positively charged antibiotic substrate.
PDB ID: 1BO4Download
MMDB ID: 8516
PDB Deposition Date: 1998/8/8
Updated in MMDB: 2012/11
Experimental Method:
x-ray diffraction
Resolution: 2.3  Å
Source Organism:
Similar Structures:
Biological Unit for 1BO4: dimeric; determined by author and by software (PISA,PQS)
Molecular Components in 1BO4
Label Count Molecule
Proteins (2 molecules)
Protein (Serratia Marcescens Aminoglycoside-3-n- Acetyltransferase)
Molecule annotation
Chemicals (3 molecules)
* Click molecule labels to explore molecular sequence information.

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