4H4J
Crystal structure of a N-acetylmuramoyl-L-alanine amidase (BACUNI_02947) from Bacteroides uniformis ATCC 8492 at 1.15 A resolution
4H4J の概要
エントリーDOI | 10.2210/pdb4h4j/pdb |
分子名称 | hypothetical protein (2 entities in total) |
機能のキーワード | pf07313 family protein, duf 1460, structural genomics, joint center for structural genomics, jcsg, protein structure initiative, psi-biology, unknown function, structural genomics unknown function |
由来する生物種 | Bacteroides uniformis |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 26898.62 |
構造登録者 | |
主引用文献 | Xu, Q.,Mengin-Lecreulx, D.,Patin, D.,Grant, J.C.,Chiu, H.J.,Jaroszewski, L.,Knuth, M.W.,Godzik, A.,Lesley, S.A.,Elsliger, M.A.,Deacon, A.M.,Wilson, I.A. Structure-guided functional characterization of DUF1460 reveals a highly specific NlpC/P60 amidase family. Structure, 22:1799-1809, 2014 Cited by PubMed Abstract: 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 Å resolution shows that AmiA is related to NlpC/P60 γ-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. PubMed: 25465128DOI: 10.1016/j.str.2014.09.018 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.15 Å) |
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