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1bgl

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[[Image:1bgl.gif|left|200px]]
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[[Image:1bgl.png|left|200px]]
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==Overview==
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{{ABSTRACT_8008071}}
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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.
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==About this Structure==
==About this Structure==
1BGL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. The following page contains interesting information on the relation of 1BGL with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb39_1.html lac Repressor]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BGL OCA].
1BGL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. The following page contains interesting information on the relation of 1BGL with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb39_1.html lac Repressor]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BGL OCA].
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==Reference==
 
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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: Matthews, B W.]]
[[Category: Matthews, B W.]]
[[Category: Zhang, X.]]
[[Category: Zhang, X.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:29:10 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jun 26 17:05:00 2008''

Revision as of 14:05, 26 June 2008

Image:1bgl.png

Template:STRUCTURE 1bgl

BETA-GALACTOSIDASE (CHAINS A-H)


Template:ABSTRACT 8008071

About this Structure

1BGL is a Single protein structure of sequence from Escherichia coli. The following page contains interesting information on the relation of 1BGL with [lac Repressor]. Full crystallographic information is available from OCA.

Page seeded by OCA on Thu Jun 26 17:05:00 2008

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