期刊
STRUCTURE
卷 22, 期 12, 页码 1799-1809出版社
CELL PRESS
DOI: 10.1016/j.str.2014.09.018
关键词
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资金
- NIH, National Institute of General Medical Sciences (NIGMS), Protein Structure Initiative [U54 GM094586]
- CNRS
- Universite Paris-Sud
- U.S. Department of Energy (DOE), Office of Science, Office of Basic Energy Sciences [DE-AC02-76SF00515]
- DOE Office of Biological and Environmental Research
- NIH, NIGMS [P41GM103393]
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [P41GM103393, U54GM094586] Funding Source: NIH RePORTER
GlcNAc-1,6-anhydro-MurNAc-tetrapeptide is a major peptidoglycan degradation intermediate and a cytotoxin. It is generated by lytic transglycosylases and further degraded and recycled by various enzymes. We have identified and characterized a highly specific N-acetylmuramoyl-L-alanine amidase (AmiA) from Bacteroides uniformis, a member of the DUF1460 protein family, that hydrolyzes GlcNAc-1,6-anhydro-MurNAc-peptide into disaccharide and stem peptide. The high-resolution apo structure at 1.15 angstrom resolution shows that AmiA is related to NlpC/P60 gamma-D-Glu-meso-diaminopimelic acid amidases and shares a common catalytic core and cysteine peptidase-like active site. AmiA has evolved structural adaptations that reconfigure the substrate recognition site. The preferred substrates for AmiA were predicted in silico based on structural and bioinformatics data, and subsequently were characterized experimentally. Further crystal structures of AmiA in complexes with GlcNAc-1,6-anhydro-MurNAc and GlcNAc have enabled us to elucidate substrate recognition and specificity. DUF1460 is highly conserved in structure and defines another amidase family.
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