1QWZ

Crystal structure of Sortase B from S. aureus complexed with MTSET

Summary for 1QWZ

• Entry DOI: 10.2210/pdb1qwz/pdb
• Related: 1QX6 1QXA
• Descriptor: NPQTN specific sortase B, NICKEL (II) ION, SULFATE ION, ... (5 entities in total)
• Functional Keywords: beta barrel, transpeptidase, hydrolase
• Biological source: Staphylococcus aureus
• Total number of polymer chains: 1
• Total formula weight: 28371.42

Authors

Zong, Y.,Mazmanian, S.K.,Schneewind, O.,Narayana, S.V. (deposition date: 2003-09-03, release date: 2004-04-06, Last modification date: 2024-04-03)

Primary citation

Zong, Y.,Mazmanian, S.K.,Schneewind, O.,Narayana, S.V.
The structure of sortase B, a cysteine transpeptidase that tethers surface protein to the Staphylococcus aureus cell wall
Structure, 12:105-112, 2004

PubMed Abstract: Many surface proteins of Gram-positive bacteria, which play important roles during the pathogenesis of human infections, are anchored to the cell wall envelope by a mechanism requiring sortases. Sortase B, a cysteine transpeptidase from Staphylococcus aureus, cleaves the C-terminal sorting signal of IsdC at the NPQTN motif and tethers the polypeptide to the pentaglycine cell wall cross-bridge. During catalysis, the active site cysteine of sortase and the cleaved substrate form an acyl intermediate, which is then resolved by the amino group of pentaglycine cross-bridges. We report here the crystal structures of SrtBDeltaN30 in complex with two active site inhibitors, MTSET and E64, and with the cell wall substrate analog tripleglycine. These structures reveal, for the first time, the active site disposition and the unique Cys-Arg catalytic machinery of the cysteine transpeptidase, and they also provide useful information for the future design of anti-infective agents against sortases.

PubMed: 14725770
DOI: 10.1016/j.str.2003.11.021

Experimental method

X-RAY DIFFRACTION (1.75 Å)