Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1TZ3

crystal structure of aminoimidazole riboside kinase complexed with aminoimidazole riboside

Summary for 1TZ3
Entry DOI10.2210/pdb1tz3/pdb
Related1TYY 1TZ6
Descriptorputative sugar kinase, POTASSIUM ION, 5-AMINOIMIDAZOLE RIBONUCLEOSIDE, ... (4 entities in total)
Functional Keywordsribokinase fold, alpha/beta, transferase
Biological sourceSalmonella typhimurium LT2
Total number of polymer chains2
Total formula weight73624.92
Authors
Zhang, Y.,Dougherty, M.,Downs, D.M.,Ealick, S.E. (deposition date: 2004-07-09, release date: 2004-10-12, Last modification date: 2024-11-13)
Primary citationZhang, Y.,Dougherty, M.,Downs, D.M.,Ealick, S.E.
Crystal Structure of an Aminoimidazole Riboside Kinase from Salmonella enterica; Implications for the Evolution of the Ribokinase Superfamily
STRUCTURE, 12:1809-1821, 2004
Cited by
PubMed Abstract: The crystal structures of a Salmonella enterica aminoimidazole riboside (AIRs) kinase, its complex with the substrate AIRs, and its complex with AIRs and an ATP analog were determined at 2.6 angstroms, 2.9 angstroms, and 2.7 angstroms, respectively. The product of the Salmonella-specific gene stm4066, AIRs kinase, is a homodimer with one active site per monomer. The core structure, consisting of an eight-stranded beta sheet flanked by eight alpha helices, indicates that AIRs kinase is a member of the ribokinase superfamily. Unlike ribokinase and adenosine kinase in this superfamily, AIRs kinase does not show significant conformational changes upon substrate binding. The active site is covered by a lid formed by residues 16-28 and 86-100. A comparison of the structure of AIRs kinase with other ribokinase superfamily members suggests that the active site lid and conformational changes that occur upon substrate binding may be advanced features in the evolution of the ribokinase superfamily.
PubMed: 15458630
DOI: 10.1016/j.str.2004.07.020
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.9 Å)
Structure validation

236963

PDB entries from 2025-06-04

PDB statisticsPDBj update infoContact PDBjnumon