1QAZ
CRYSTAL STRUCTURE OF ALGINATE LYASE A1-III FROM SPHINGOMONAS SPECIES A1 AT 1.78A RESOLUTION
Summary for 1QAZ
| Entry DOI | 10.2210/pdb1qaz/pdb |
| Descriptor | PROTEIN (ALGINATE LYASE A1-III), SULFATE ION (3 entities in total) |
| Functional Keywords | alginate lyase, crystals, lyase |
| Biological source | Sphingomonas sp. |
| Total number of polymer chains | 1 |
| Total formula weight | 39841.72 |
| Authors | Yoon, H.-J. (deposition date: 1999-04-08, release date: 1999-07-19, Last modification date: 2024-11-06) |
| Primary citation | Yoon, H.J.,Mikami, B.,Hashimoto, W.,Murata, K. Crystal structure of alginate lyase A1-III from Sphingomonas species A1 at 1.78 A resolution. J.Mol.Biol., 290:505-514, 1999 Cited by PubMed Abstract: The three-dimensional structure of alginate lyase A1-III (ALYIII) from a Sphingomonas species A1 was determined by X-ray crystallography. The enzyme was crystallized by the hanging-drop vapour-diffusion method in the presence of 49% ammonium sulfate at 20 degrees C. The crystals are monoclinic and belong to the space group C2 with unit cell dimensions of a=49.18 A, b=93.08 A, c=82.10 A and beta=104.12 degrees. There was one molecule of alginate lyase in the asymmetric unit of the crystal. The diffraction data up to 1. 71 A were collected with Rsymof 5.0%. The crystal structure of ALYIII was solved by the multiple isomorphous replacement method and refined at 1.78 A resolution using X-PLOR with a final R -factor of 18.0% for 10.0 to 1.78 A resolution data. The refined model of ALYIII contained 351 amino acid residues, 299 water molecules and two sulfate ions. The three-dimensional structure of ALYIII was abundant in helices and had a deep tunnel-like cleft in a novel (alpha6/alpha5)-barrel structure, which was similar to the (alpha6/alpha6)-barrel found in glucoamylase and cellulase. This structure presented the possibility that alginate molecules might penetrate into the cleft to interact with the catalytic site of ALYIII. PubMed: 10390348DOI: 10.1006/jmbi.1999.2883 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.78 Å) |
Structure validation
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