4F4M

Structure of the type VI peptidoglycan amidase effector Tse1 (C30A) from Pseudomonas aeruginosa

Summary for 4F4M

• Entry DOI: 10.2210/pdb4f4m/pdb
• Related: 4EOB
• Descriptor: papain peptidoglycan amidase effector Tse1 (1 entity in total)
• Functional Keywords: papain peptidoglycan amidase effector, amidase, tsi1, hydrolase regulator
• Biological source: Pseudomonas aeruginosa
• Total number of polymer chains: 4
• Total formula weight: 69021.96

Authors

Chou, S.,Mougous, J.D. (deposition date: 2012-05-10, release date: 2012-05-30, Last modification date: 2024-10-30)

Primary citation

Chou, S.,Bui, N.K.,Russell, A.B.,Lexa, K.W.,Gardiner, T.E.,LeRoux, M.,Vollmer, W.,Mougous, J.D.
Structure of a peptidoglycan amidase effector targeted to Gram-negative bacteria by the type VI secretion system.
Cell Rep, 1:656-664, 2012

PubMed Abstract: The target range of a bacterial secretion system can be defined by effector substrate specificity or by the efficacy of effector delivery. Here, we report the crystal structure of Tse1, a type VI secretion (T6S) bacteriolytic amidase effector from Pseudomonas aeruginosa. Consistent with its role as a toxin, Tse1 has a more accessible active site than related housekeeping enzymes. The activity of Tse1 against isolated peptidoglycan shows its capacity to act broadly against Gram-negative bacteria and even certain Gram-positive species. Studies with intact cells indicate that Gram-positive bacteria can remain vulnerable to Tse1 despite cell wall modifications. However, interbacterial competition studies demonstrate that Tse1-dependent lysis is restricted to Gram-negative targets. We propose that the previously observed specificity for T6S against Gram-negative bacteria is a consequence of high local effector concentration achieved by T6S-dependent targeting to its site of action rather than inherent effector substrate specificity.

PubMed: 22813741
DOI: 10.1016/j.celrep.2012.05.016

Experimental method

X-RAY DIFFRACTION (2.677 Å)