3TBE

The crystal structure of the complex of Streptococcus agalactiae sortase C1 and MTSET

Summary for 3TBE

• Entry DOI: 10.2210/pdb3tbe/pdb
• Related: 3TB7
• Descriptor: Sortase family protein, 2-(TRIMETHYLAMMONIUM)ETHYL THIOL, SULFATE ION, ... (5 entities in total)
• Functional Keywords: beta-barrel, pili-biogenesis, 2-(trimethylammonium)-ethyl-methanethiosulfonate bromide, hydrolase
• Biological source: Streptococcus agalactiae serogroup V
• Total number of polymer chains: 6
• Total formula weight: 155888.55

Authors

Khare, B. (deposition date: 2011-08-05, release date: 2011-10-26, Last modification date: 2024-11-20)

Primary citation

Khare, B.,Fu, Z.Q.,Huang, I.H.,Ton-That, H.,Narayana, S.V.
The Crystal Structure Analysis of Group B Streptococcus Sortase C1: A Model for the "Lid" Movement upon Substrate Binding.
J.Mol.Biol., 414:563-577, 2011

PubMed Abstract: A unique feature of the class-C-type sortases, enzymes essential for Gram-positive pilus biogenesis, is the presence of a flexible "lid" anchored in the active site. However, the mechanistic details of the "lid" displacement, suggested to be a critical prelude for enzyme catalysis, are not yet known. This is partly due to the absence of enzyme-substrate and enzyme-inhibitor complex crystal structures. We have recently described the crystal structures of the Streptococcus agalactiae SAG2603 V/R sortase SrtC1 in two space groups (type II and type III) and that of its "lid" mutant and proposed a role of the "lid" as a protector of the active-site hydrophobic environment. Here, we report the crystal structures of SAG2603 V/R sortase C1 in a different space group (type I) and that of its complex with a small-molecule cysteine protease inhibitor. We observe that the catalytic Cys residue is covalently linked to the small-molecule inhibitor without lid displacement. However, the type I structure provides a view of the sortase SrtC1 lid displacement while having structural elements similar to a substrate sorting motif suitably positioned in the active site. We propose that these major conformational changes seen in the presence of a substrate mimic in the active site may represent universal features of class C sortase substrate recognition and enzyme activation.

PubMed: 22033482
DOI: 10.1016/j.jmb.2011.10.017

Experimental method

X-RAY DIFFRACTION (2.85 Å)