1LBA
THE STRUCTURE OF BACTERIOPHAGE T7 LYSOZYME, A ZINC AMIDASE AND AN INHIBITOR OF T7 RNA POLYMERASE
Summary for 1LBA
| Entry DOI | 10.2210/pdb1lba/pdb |
| Descriptor | T7 LYSOZYME, ZINC ION (3 entities in total) |
| Functional Keywords | hydrolase(acting on linear amides) |
| Biological source | Enterobacteria phage T7 |
| Total number of polymer chains | 1 |
| Total formula weight | 16409.89 |
| Authors | Cheng, X. (deposition date: 1993-12-22, release date: 1994-04-30, Last modification date: 2024-02-14) |
| Primary citation | Cheng, X.,Zhang, X.,Pflugrath, J.W.,Studier, F.W. The structure of bacteriophage T7 lysozyme, a zinc amidase and an inhibitor of T7 RNA polymerase. Proc.Natl.Acad.Sci.USA, 91:4034-4038, 1994 Cited by PubMed Abstract: The lysozyme of bacteriophage T7 is a bifunctional protein that cuts amide bonds in the bacterial cell wall and binds to and inhibits transcription by T7 RNA polymerase. The structure of a mutant T7 lysozyme has been determined by x-ray crystallography and refined at 2.2-A resolution. The protein folds into an alpha/beta-sheet structure that has a prominent cleft. A zinc atom is located in the cleft, bound directly to three amino acids and, through a water molecule, to a fourth. Zinc is required for amidase activity but not for inhibition of T7 RNA polymerase. Alignment of the zinc ligands of T7 lysozyme with those of carboxypeptidase A and thermolysin suggests structural similarity among the catalytic sites for the amidase and these zinc proteases. Mutational analysis identified presumed catalytic residues for amidase activity within the cleft and a surface that appears to be the site of binding to T7 RNA polymerase. Binding of T7 RNA polymerase inhibits amidase activity. PubMed: 8171031DOI: 10.1073/pnas.91.9.4034 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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