1bgm
From Proteopedia
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| - | [[Image:1bgm.jpg|left|200px]] | + | [[Image:1bgm.jpg|left|200px]] |
| - | + | ||
| - | '''BETA-GALACTOSIDASE (CHAINS I-P)''' | + | {{Structure |
| + | |PDB= 1bgm |SIZE=350|CAPTION= <scene name='initialview01'>1bgm</scene>, resolution 2.5Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Beta-galactosidase Beta-galactosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.23 3.2.1.23] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''BETA-GALACTOSIDASE (CHAINS I-P)''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1BGM is a [ | + | 1BGM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BGM OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8008071 8008071] |
[[Category: Beta-galactosidase]] | [[Category: Beta-galactosidase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
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[[Category: hydrolase (o-glycosyl)]] | [[Category: hydrolase (o-glycosyl)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:10:50 2008'' |
Revision as of 08:10, 20 March 2008
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| , resolution 2.5Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Beta-galactosidase, with EC number 3.2.1.23 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
BETA-GALACTOSIDASE (CHAINS I-P)
Overview
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.
About this Structure
1BGM is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Mar 20 10:10:50 2008
