3pbg: Difference between revisions
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[[Image:3pbg.jpg|left|200px]] | [[Image:3pbg.jpg|left|200px]] | ||
'''6-PHOSPHO-BETA-GALACTOSIDASE FORM-C''' | {{Structure | ||
|PDB= 3pbg |SIZE=350|CAPTION= <scene name='initialview01'>3pbg</scene>, resolution 2.7Å | |||
|SITE= <scene name='pdbsite=ACA:Catalytic+Residues'>ACA</scene>, <scene name='pdbsite=ACB:Catalytic+Residues'>ACB</scene>, <scene name='pdbsite=PHA:Phosphate+Binding+Site'>PHA</scene> and <scene name='pdbsite=PHB:Phosphate+Binding+Site'>PHB</scene> | |||
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/6-phospho-beta-galactosidase 6-phospho-beta-galactosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.85 3.2.1.85] | |||
|GENE= LACG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1358 Lactococcus lactis]) | |||
}} | |||
'''6-PHOSPHO-BETA-GALACTOSIDASE FORM-C''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
3PBG is a [ | 3PBG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Lactococcus_lactis Lactococcus lactis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PBG OCA]. | ||
==Reference== | ==Reference== | ||
Crystal structures and mechanism of 6-phospho-beta-galactosidase from Lactococcus lactis., Wiesmann C, Hengstenberg W, Schulz GE, J Mol Biol. 1997 Jun 27;269(5):851-60. PMID:[http:// | Crystal structures and mechanism of 6-phospho-beta-galactosidase from Lactococcus lactis., Wiesmann C, Hengstenberg W, Schulz GE, J Mol Biol. 1997 Jun 27;269(5):851-60. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9223646 9223646] | ||
[[Category: 6-phospho-beta-galactosidase]] | [[Category: 6-phospho-beta-galactosidase]] | ||
[[Category: Lactococcus lactis]] | [[Category: Lactococcus lactis]] | ||
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[[Category: hydrolase]] | [[Category: hydrolase]] | ||
''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 19:06:20 2008'' | ||
Revision as of 20:06, 20 March 2008
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| , resolution 2.7Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , and | ||||||
| Ligands: | |||||||
| Gene: | LACG (Lactococcus lactis) | ||||||
| Activity: | 6-phospho-beta-galactosidase, with EC number 3.2.1.85 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
6-PHOSPHO-BETA-GALACTOSIDASE FORM-C
OverviewOverview
The initial structural model of 6-phospho-beta-galactosidase from Lactococcus lactis was refined to an R-factor of 16.4% (R[free] = 23.6%) to 2.3 A resolution (1 A = 0.1 nm), and the structures of three other crystal forms were solved by molecular replacement. The four structural models are essentially identical. The catalytic center of the enzyme is approximately at the mass center of the molecule and can only be reached through a 20 A long channel, which is observed with an "open" or "closed" entrance. The closed entrance is probably too small for the educt lactose-6-phosphate to enter, but large enough for the first product glucose to leave. Among the presented structures is a complex between an almost inactive mutant and the second product galactose-6-phosphate, which is exclusively bound at side-chains. A superposition (onto the native enzyme) of galactose-6-phosphate as bound to the mutant suggests the geometry of a postulated covalent intermediate. The binding mode of the educt was modeled, starting from the bound galactose-6-phosphate. A tightly fixed tryptophan is used as a chopping-board for splitting the disaccharide, and several other aromatic residues in the active center cavity are likely to participate in substrate transport/binding.
About this StructureAbout this Structure
3PBG is a Single protein structure of sequence from Lactococcus lactis. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structures and mechanism of 6-phospho-beta-galactosidase from Lactococcus lactis., Wiesmann C, Hengstenberg W, Schulz GE, J Mol Biol. 1997 Jun 27;269(5):851-60. PMID:9223646
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