Sandbox Reserved 1800

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Function of your protein

The function of this protein is to catalyze the formation of dipeptide products in gram-positive bacteria

Biological relevance and broader implications

Enzymes involved in the amino acid metabolism of Staphylococcus aureus are being studied as potential targets for new antibiotics. One group of enzymes, called L-amino acid ligases (LALs), which catalyze the formation of dipeptide products in Gram-positive bacteria, have not been investigated in S. aureus until now. The putative ATP-grasp enzyme SAOUHSC_02373 from S. aureus NCTC 8325 was found to be a novel LAL with high selectivity for !-aspartate and L-methionine substrates, forming an L-aspartyl–L-methionine dipeptide. It was named L-aspartate–L-methionine ligase (LdmS). The mechanism of LdmS was investigated using X-ray crystallography, molecular modeling, and site-directed mutagenesis. LdmS was found to share a similar mechanism to other ATP-grasp enzymes but possesses a unique active site architecture that confers selectivity for !-Asp and L-Met substrates. Phylogenetic analysis showed that LdmS homologs are highly conserved in Staphylococcus and closely related Gram-positive Firmicutes. Genetic analysis upstream of the ldmS operon revealed several trans-acting regulatory elements associated with the control of Met and Cys metabolism, supporting a role for LdmS in Staphylococcal sulfur amino acid metabolism.

Important Ligands

The important ligands are citric acid (CIT), Chloride ion (CL), Magnesium ion (MG), and Sodium ion (NA). You can see them clearly .

Another important ligand in this protein is ADP that you can see .

Structural highlights

of 50/50 beta sheets to alpha helixes. You can see the round globular shape with a clear central opening.

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