2RUI

Solution Structure of the Bacillus anthracis Sortase A-substrate Complex

Summary for 2RUI

• Entry DOI: 10.2210/pdb2rui/pdb
• NMR Information: BMRB: 11570
• Related PRD ID: PRD_001241
• Descriptor: LPXTG-site transpeptidase family protein, Boc-LPAT* (2 entities in total)
• Functional Keywords: sortase, srta, transpeptidase, hydrolase-hydrolase substrate complex, hydrolase/hydrolase substrate
• Biological source: Bacillus anthracis str. Sterne (anthrax, anthrax bacterium); More
• Total number of polymer chains: 2
• Total formula weight: 17613.05

Authors

Chan, A.H.,Yi, S.,Jung, M.E.,Clubb, R.T. (deposition date: 2014-06-22, release date: 2015-09-09, Last modification date: 2023-11-15)

Primary citation

Chan, A.H.,Yi, S.W.,Terwilliger, A.L.,Maresso, A.W.,Jung, M.E.,Clubb, R.T.
Structure of the Bacillus anthracis Sortase A Enzyme Bound to Its Sorting Signal: A FLEXIBLE AMINO-TERMINAL APPENDAGE MODULATES SUBSTRATE ACCESS.
J.Biol.Chem., 290:25461-25474, 2015

PubMed Abstract: The endospore forming bacterium Bacillus anthracis causes lethal anthrax disease in humans and animals. The ability of this pathogen to replicate within macrophages is dependent upon the display of bacterial surface proteins attached to the cell wall by the B. anthracis Sortase A ((Ba)SrtA) enzyme. Previously, we discovered that the class A (Ba)SrtA sortase contains a unique N-terminal appendage that wraps around the body of the protein to contact the active site of the enzyme. To gain insight into its function, we determined the NMR structure of (Ba)SrtA bound to a LPXTG sorting signal analog. The structure, combined with dynamics, kinetics, and whole cell protein display data suggest that the N terminus modulates substrate access to the enzyme. We propose that it may increase the efficiency of protein display by reducing the unproductive hydrolytic cleavage of enzyme-protein covalent intermediates that form during the cell wall anchoring reaction. Notably, a key active site loop (β7/β8 loop) undergoes a disordered to ordered transition upon binding the sorting signal, potentially facilitating recognition of lipid II.

PubMed: 26324714
DOI: 10.1074/jbc.M115.670984

Experimental method

SOLUTION NMR