ArticleThe Journal of biological chemistry2010
Crystal structure of Staphylococcus aureus metallopeptidase (Sapep) reveals large domain motions between the manganese-bound and apo-states.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 31 citations in OpenAlex.
- A SecA-associated protease modulates the extent of surface display of staphylococcal protein A.Journal of bacteriology · 2025Article
- Identification of a staphylococcal dipeptidase involved in the production of human body odor.The Journal of biological chemistry · 2024Article
- Novel aminoacylases from Streptomyces griseus DSM 40236 and their recombinant production in Streptomyces lividans.FEBS open bio · 2023Article
- Massively parallel, computationally guided design of a proenzyme.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Engineering carboxypeptidase G2 circular permutations for the design of an autoinhibited enzyme.Protein engineering, design & selection : PEDS · 2017Article
- Evidence for an essential role of intradimer interaction in catalytic function of carnosine dipeptidase II using electrospray-ionization mass spectrometry.Protein science : a publication of the Protein Society · 2016Article
- Article
- Crystallization and preliminary X-ray diffraction studies of Staphylococcus aureus homoserine dehydrogenase.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013Article
- Structure of an amidohydrolase, SACOL0085, from methicillin-resistant Staphylococcus aureus COL.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013Article
- Mutational and structural analysis of L-N-carbamoylase reveals new insights into a peptidase M20/M25/M40 family member.Journal of bacteriology · 2012Article
- A mutation in the PP2C phosphatase gene in a Staphylococcus aureus USA300 clinical isolate with reduced susceptibility to vancomycin and daptomycin.Antimicrobial agents and chemotherapy · 2012Article
- Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of succinyl-diaminopimelate desuccinylase (Rv1202, DapE) from Mycobacterium tuberculosis.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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.
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