Summary for 1UUZ
| Entry DOI | 10.2210/pdb1uuz/pdb |
| Related | 132L 193L 194L 1A2Y 1AKI 1AT5 1AT6 1AZF 1B0D 1B2K 1BGI 1BHZ 1BVK 1BVX 1BWH 1BWI 1BWJ 1C08 1C10 1DPW 1DPX 1DQJ 1E8L 1F0W 1F10 1F3J 1FDL 1FLQ 1FLU 1FLW 1FLY 1FN5 1G7H 1G7I 1G7J 1G7L 1G7M 1GPQ 1GWD 1GXV 1GXX 1H6M 1H87 1HC0 1HEL 1HEM 1HEN 1HEO 1HEP 1HEQ 1HER 1HEW 1HF4 1HSW 1HSX 1IC4 1IC5 1IC7 1IEE 1IO5 1IOQ 1IOR 1IOS 1IOT 1IR7 1IR8 1IR9 1J1O 1J1P 1J1X 1JA2 1JA4 1JA6 1JA7 1JIS 1JIT 1JIY 1JJ0 1JJ1 1JJ3 1JPO 1JTO 1JTT 1KIP 1KIQ 1KIR 1KXW 1KXX 1KXY 1LCN 1LJ3 1LJ4 1LJE 1LJF 1LJG 1LJH 1LJI 1LJJ 1LJK 1LKR 1LKS 1LMA 1LPI 1LSA 1LSB 1LSC 1LSD 1LSE 1LSF 1LSG 1LSM 1LSN 1LSY 1LSZ 1LYO 1LYS 1LYZ 1LZ8 1LZ9 1LZA 1LZB 1LZC 1LZD 1LZE 1LZG 1LZH 1LZN 1LZT 1MEL 1MLC 1N4F 1NBY 1NBZ 1NDG 1NDM 1PS5 1QIO 1QTK 1RCM 1RFP 1UC0 1UCO 1UIA 1UIB 1UIC 1UID 1UIE 1UIF 1UIG 1UIH 1VFB 1XEI 1XEJ 1XEK 2CDS 2HFM 2IFF 2LYM 2LYO 2LYZ 2LZH 2LZT 3HFL 3HFM 3LYM 3LYO 3LYT 3LYZ 3LZT 4LYM 4LYO 4LYT 4LYZ 4LZT 5LYM 5LYT 5LYZ 6LYT 6LYZ 7LYZ 8LYZ |
| Descriptor | INHIBITOR OF VERTEBRATE LYSOZYME, LYSOZYME C (3 entities in total) |
| Functional Keywords | hydrolase/inhibitor, lysozyme-inhibitor complex, ivy, type-c lysozyme inhibitor, lysozyme, hydrolase, glycosidase, hydrolase-inhibitor complex |
| Biological source | PSEUDOMONAS AERUGINOSA More |
| Cellular location | Secreted: P00698 |
| Total number of polymer chains | 4 |
| Total formula weight | 59760.98 |
| Authors | Abergel, C.,Lembo, F.,Byrne, D.,Maza, C.,Claverie, J.M. (deposition date: 2004-01-12, release date: 2004-01-14, Last modification date: 2023-12-13) |
| Primary citation | Abergel, C.,Monchois, V.,Byrne, D.,Chenivesse, S.,Lembo, F.,Lazzaroni, J.-C.,Claverie, J.M. Structure and Evolution of the Ivy Protein Family, Unexpected Lysozyme Inhibitors in Gram-Negative Bacteria. Proc.Natl.Acad.Sci.USA, 104:6394-, 2007 Cited by PubMed Abstract: Part of an ancestral bactericidal system, vertebrate C-type lysozyme targets the peptidoglycan moiety of bacterial cell walls. We report the crystal structure of a protein inhibitor of C-type lysozyme, the Escherichia coli Ivy protein, alone and in complex with hen egg white lysozyme. Ivy exhibits a novel fold in which a protruding five-residue loop appears essential to its inhibitory effect. This feature guided the identification of Ivy orthologues in other Gram-negative bacteria. The structure of the evolutionary distant Pseudomonas aeruginosa Ivy orthologue was also determined in complex with hen egg white lysozyme, and its antilysozyme activity was confirmed. Ivy expression protects porous cell-wall E. coli mutants from the lytic effect of lysozyme, suggesting that it is a response against the permeabilizing effects of the innate vertebrate immune system. As such, Ivy acts as a virulence factor for a number of Gram-negative bacteria-infecting vertebrates. PubMed: 17405861DOI: 10.1073/PNAS.0611019104 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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