3KHZ

Crystal Structure of R350A mutant of Staphylococcus aureus metallopeptidase (Sapep/DapE) in the apo-form

Summary for 3KHZ

• Entry DOI: 10.2210/pdb3khz/pdb
• Related: 3KHX 3KI9
• Descriptor: Putative dipeptidase SACOL1801 (2 entities in total)
• Functional Keywords: r350a mutant-dipeptidase, dape, metallopeptidase, dipeptidase, hydrolase, metal-binding, metalloprotease, protease
• Biological source: Staphylococcus aureus
• Total number of polymer chains: 2
• Total formula weight: 110507.08

Authors

Girish, T.S.,Gopal, B. (deposition date: 2009-10-31, release date: 2010-07-07, Last modification date: 2024-11-20)

Primary citation

Girish, T.S.,Gopal, B.
Crystal structure of Staphylococcus aureus metallopeptidase (Sapep) reveals large domain motions between the manganese-bound and apo-states
J.Biol.Chem., 285:29406-29415, 2010

PubMed Abstract: Proteases belonging to the M20 family are characterized by diverse substrate specificity and participate in several metabolic pathways. The Staphylococcus aureus metallopeptidase, Sapep, is a member of the aminoacylase-I/M20 protein family. This protein is a Mn(2+)-dependent dipeptidase. The crystal structure of this protein in the Mn(2+)-bound form and in the open, metal-free state suggests that large interdomain movements could potentially regulate the activity of this enzyme. We note that the extended inactive conformation is stabilized by a disulfide bond in the vicinity of the active site. Although these cysteines, Cys(155) and Cys(178), are not active site residues, the reduced form of this enzyme is substantially more active as a dipeptidase. These findings acquire further relevance given a recent observation that this enzyme is only active in methicillin-resistant S. aureus. The structural and biochemical features of this enzyme provide a template for the design of novel methicillin-resistant S. aureus-specific therapeutics.

PubMed: 20610394
DOI: 10.1074/jbc.M110.147579

Experimental method

X-RAY DIFFRACTION (2.5 Å)