1bgl | pdb_00001bgl

BETA-GALACTOSIDASE (CHAINS A-H)

spinqualitylabelsall models 1bgl, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1bgl is a 8 chain structure with sequence from Escherichia coli. The March 2003 RCSB PDB Molecule of the Month feature on lac Repressor by David S. Goodsell is 10.2210/rcsb_pdb/mom_2003_3. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: MG Related: 1bgm Activity: Beta-galactosidase, with EC number 3.2.1.23 Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The beta-galactosidase from Escherichia coli was instrumental in the development of the operon model, and today is one of the most commonly used enzymes in molecular biology. Here we report the structure of this protein and show that it is a tetramer with 222-point symmetry. The 1,023-amino-acid polypeptide chain folds into five sequential domains, with an extended segment at the amino terminus. The participation of this amino-terminal segment in a subunit interface, coupled with the observation that each active site is made up of elements from two different subunits, provides a structural rationale for the phenomenon of alpha-complementation. The structure represents the longest polypeptide chain for which an atomic structure has been determined. Our results show that it is possible successfully to study non-viral protein crystals with unit cell dimensions in excess of 500 A and with relative molecular masses in the region of 2,000K per asymmetric unit. Non-crystallographic symmetry averaging proved to be a very powerful tool in the structure determination, as has been shown in other contexts. Three-dimensional structure of beta-galactosidase from E. coli.,Jacobson RH, Zhang XJ, DuBose RF, Matthews BW Nature. 1994 Jun 30;369(6483):761-6. PMID:8008071 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Galactosidase

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