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1bgl

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[[Image:1bgl.gif|left|200px]]
[[Image:1bgl.gif|left|200px]]
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{{Structure
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|PDB= 1bgl |SIZE=350|CAPTION= <scene name='initialview01'>1bgl</scene>, resolution 2.5&Aring;
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The line below this paragraph, containing "STRUCTURE_1bgl", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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|GENE=
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{{STRUCTURE_1bgl| PDB=1bgl | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bgl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bgl OCA], [http://www.ebi.ac.uk/pdbsum/1bgl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bgl RCSB]</span>
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}}
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'''BETA-GALACTOSIDASE (CHAINS A-H)'''
'''BETA-GALACTOSIDASE (CHAINS A-H)'''
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: lac Repressor]]
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[[Category: Lac Repressor]]
[[Category: Dubose, R F.]]
[[Category: Dubose, R F.]]
[[Category: Jacobson, R H.]]
[[Category: Jacobson, R H.]]
[[Category: Matthews, B W.]]
[[Category: Matthews, B W.]]
[[Category: Zhang, X.]]
[[Category: Zhang, X.]]
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[[Category: hydrolase (o-glycosyl)]]
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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 Sun Mar 30 19:00:27 2008''
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Revision as of 08:29, 2 May 2008

Image:1bgl.gif

Template:STRUCTURE 1bgl

BETA-GALACTOSIDASE (CHAINS A-H)


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

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.

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 Fri May 2 11:29:10 2008

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