1jz2: Difference between revisions
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[[Image:1jz2.gif|left|200px]] | [[Image:1jz2.gif|left|200px]] | ||
'''E. COLI (lacZ) BETA-GALACTOSIDASE-TRAPPED 2-F-GALACTOSYL-ENZYME INTERMEDIATE (ORTHORHOMBIC)''' | {{Structure | ||
|PDB= 1jz2 |SIZE=350|CAPTION= <scene name='initialview01'>1jz2</scene>, resolution 2.10Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=2FG:2-FLUORO-2-DEOXY-BETA-D-GALACTOPYRANOSE'>2FG</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene> and <scene name='pdbligand=BTB:2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>BTB</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= lacZ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |||
}} | |||
'''E. COLI (lacZ) BETA-GALACTOSIDASE-TRAPPED 2-F-GALACTOSYL-ENZYME INTERMEDIATE (ORTHORHOMBIC)''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1JZ2 is a [ | 1JZ2 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=1JZ2 OCA]. | ||
==Reference== | ==Reference== | ||
A structural view of the action of Escherichia coli (lacZ) beta-galactosidase., Juers DH, Heightman TD, Vasella A, McCarter JD, Mackenzie L, Withers SG, Matthews BW, Biochemistry. 2001 Dec 11;40(49):14781-94. PMID:[http:// | A structural view of the action of Escherichia coli (lacZ) beta-galactosidase., Juers DH, Heightman TD, Vasella A, McCarter JD, Mackenzie L, Withers SG, Matthews BW, Biochemistry. 2001 Dec 11;40(49):14781-94. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11732897 11732897] | ||
[[Category: Beta-galactosidase]] | [[Category: Beta-galactosidase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
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[[Category: tim barrel (alpha/beta barrel)]] | [[Category: tim barrel (alpha/beta barrel)]] | ||
''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 12:10:23 2008'' | ||
Revision as of 13:10, 20 March 2008
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| , resolution 2.10Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , and | ||||||
| Gene: | lacZ (Escherichia coli) | ||||||
| Activity: | Beta-galactosidase, with EC number 3.2.1.23 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
E. COLI (lacZ) BETA-GALACTOSIDASE-TRAPPED 2-F-GALACTOSYL-ENZYME INTERMEDIATE (ORTHORHOMBIC)
OverviewOverview
The structures of a series of complexes designed to mimic intermediates along the reaction coordinate for beta-galactosidase are presented. These complexes clarify and enhance previous proposals regarding the catalytic mechanism. The nucleophile, Glu537, is seen to covalently bind to the galactosyl moiety. Of the two potential acids, Mg(2+) and Glu461, the latter is in better position to directly assist in leaving group departure, suggesting that the metal ion acts in a secondary role. A sodium ion plays a part in substrate binding by directly ligating the galactosyl 6-hydroxyl. The proposed reaction coordinate involves the movement of the galactosyl moiety deep into the active site pocket. For those ligands that do bind deeply there is an associated conformational change in which residues within loop 794-804 move up to 10 A closer to the site of binding. In some cases this can be inhibited by the binding of additional ligands. The resulting restricted access to the intermediate helps to explain why allolactose, the natural inducer for the lac operon, is the preferred product of transglycosylation.
About this StructureAbout this Structure
1JZ2 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
A structural view of the action of Escherichia coli (lacZ) beta-galactosidase., Juers DH, Heightman TD, Vasella A, McCarter JD, Mackenzie L, Withers SG, Matthews BW, Biochemistry. 2001 Dec 11;40(49):14781-94. PMID:11732897
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