4UZ2
Crystal structure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus
Summary for 4UZ2
| Entry DOI | 10.2210/pdb4uz2/pdb |
| Related | 4UZ3 4XCM |
| Descriptor | CELL WALL-BINDING ENDOPEPTIDASE-RELATED PROTEIN (2 entities in total) |
| Functional Keywords | hydrolase |
| Biological source | THERMUS THERMOPHILUS HB8 |
| Total number of polymer chains | 4 |
| Total formula weight | 43886.00 |
| Authors | Wong, J.E.M.M.,Blaise, M. (deposition date: 2014-09-04, release date: 2015-01-14, Last modification date: 2024-05-08) |
| Primary citation | Wong, J.E.M.M.,Midtgaard, S.R.,Gysel, K.,Thygesen, M.B.,Sorensen, K.K.,Jensen, K.J.,Stougaard, J.,Thirup, S.,Blaise, M. An Intermolecular Binding Mechanism Involving Multiple Lysm Domains Mediates Carbohydrate Recognition by an Endopeptidase. Acta Crystallogr.,Sect.D, 71:592-, 2015 Cited by PubMed Abstract: LysM domains, which are frequently present as repetitive entities in both bacterial and plant proteins, are known to interact with carbohydrates containing N-acetylglucosamine (GlcNAc) moieties, such as chitin and peptidoglycan. In bacteria, the functional significance of the involvement of multiple LysM domains in substrate binding has so far lacked support from high-resolution structures of ligand-bound complexes. Here, a structural study of the Thermus thermophilus NlpC/P60 endopeptidase containing two LysM domains is presented. The crystal structure and small-angle X-ray scattering solution studies of this endopeptidase revealed the presence of a homodimer. The structure of the two LysM domains co-crystallized with N-acetyl-chitohexaose revealed a new intermolecular binding mode that may explain the differential interaction between LysM domains and short or long chitin oligomers. By combining the structural information with the three-dimensional model of peptidoglycan, a model suggesting how protein dimerization enhances the recognition of peptidoglycan is proposed. PubMed: 25760608DOI: 10.1107/S139900471402793X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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