2HTA
Crystal Structure of a putative mutarotase (YeaD) from Salmonella typhimurium in orthorhombic form
Summary for 2HTA
| Entry DOI | 10.2210/pdb2hta/pdb |
| Related | 1jov 1l7k 1lur 1snz 1z45 |
| Descriptor | Putative enzyme related to aldose 1-epimerase, SULFATE ION, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | salmonella typhimurium, carbohydrate, aldose 1-epimerase, mutarotase, yead, galm, sugar phosphate, isomerase |
| Biological source | Salmonella typhimurium |
| Total number of polymer chains | 2 |
| Total formula weight | 68971.95 |
| Authors | Chittori, S.,Simanshu, D.K.,Savithri, H.S.,Murthy, M.R.N. (deposition date: 2006-07-25, release date: 2007-01-23, Last modification date: 2023-08-30) |
| Primary citation | Chittori, S.,Simanshu, D.K.,Savithri, H.S.,Murthy, M.R. Structure of the putative mutarotase YeaD from Salmonella typhimurium: structural comparison with galactose mutarotases. Acta Crystallogr.,Sect.D, 63:197-205, 2007 Cited by PubMed Abstract: Salmonella typhimurium YeaD (stYeaD), annotated as a putative aldose 1-epimerase, has a very low sequence identity to other well characterized mutarotases. Sequence analysis suggested that the catalytic residues and a few of the substrate-binding residues of galactose mutarotases (GalMs) are conserved in stYeaD. Determination of the crystal structure of stYeaD in an orthorhombic form at 1.9 A resolution and in a monoclinic form at 2.5 A resolution revealed this protein to adopt the beta-sandwich fold similar to GalMs. Structural comparison of stYeaD with GalMs has permitted the identification of residues involved in catalysis and substrate binding. In spite of the similar fold and conservation of catalytic residues, minor but significant differences were observed in the substrate-binding pocket. These analyses pointed out the possible role of Arg74 and Arg99, found only in YeaD-like proteins, in ligand anchoring and suggested that the specificity of stYeaD may be distinct from those of GalMs. PubMed: 17242513DOI: 10.1107/S090744490604618X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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