1tg7: Difference between revisions
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|PDB= 1tg7 |SIZE=350|CAPTION= <scene name='initialview01'>1tg7</scene>, resolution 1.90Å | |PDB= 1tg7 |SIZE=350|CAPTION= <scene name='initialview01'>1tg7</scene>, resolution 1.90Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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] | |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> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1bgl|1BGL]], [[1kwg|1KWG]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tg7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tg7 OCA], [http://www.ebi.ac.uk/pdbsum/1tg7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tg7 RCSB]</span> | |||
}} | }} | ||
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==About this Structure== | ==About this Structure== | ||
1TG7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ | 1TG7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Penicillium_sp. Penicillium sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TG7 OCA]. | ||
==Reference== | ==Reference== | ||
Crystal structures of beta-galactosidase from Penicillium sp. and its complex with galactose., Rojas AL, Nagem RA, Neustroev KN, Arand M, Adamska M, Eneyskaya EV, Kulminskaya AA, Garratt RC, Golubev AM, Polikarpov I, J Mol Biol. 2004 Nov 5;343(5):1281-92. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15491613 15491613] | Crystal structures of beta-galactosidase from Penicillium sp. and its complex with galactose., Rojas AL, Nagem RA, Neustroev KN, Arand M, Adamska M, Eneyskaya EV, Kulminskaya AA, Garratt RC, Golubev AM, Polikarpov I, J Mol Biol. 2004 Nov 5;343(5):1281-92. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15491613 15491613] | ||
[[Category: Beta-galactosidase]] | [[Category: Beta-galactosidase]] | ||
[[Category: Penicillium | [[Category: Penicillium sp.]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Adamska, M.]] | [[Category: Adamska, M.]] | ||
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[[Category: Polikarpov, I.]] | [[Category: Polikarpov, I.]] | ||
[[Category: Rojas, A L.]] | [[Category: Rojas, A L.]] | ||
[[Category: family gh35]] | [[Category: family gh35]] | ||
[[Category: glycoprotein]] | [[Category: glycoprotein]] | ||
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[[Category: tim barrel domain]] | [[Category: tim barrel domain]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:55:39 2008'' | ||
Revision as of 23:55, 30 March 2008
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| , resolution 1.90Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , , | ||||||
| Activity: | Beta-galactosidase, with EC number 3.2.1.23 | ||||||
| Related: | 1BGL, 1KWG
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Native structure of beta-galactosidase from Penicillium sp.
OverviewOverview
Beta-galactosidases catalyze the hydrolysis of beta(1-3) and beta(1-4) galactosyl bonds in oligosaccharides as well as the inverse reaction of enzymatic condensation and transglycosylation. Here we report the crystallographic structures of Penicillium sp. beta-galactosidase and its complex with galactose solved by the SIRAS quick cryo-soaking technique at 1.90 A and 2.10 A resolution, respectively. The amino acid sequence of this 120 kDa protein was first assigned putatively on the basis of inspection of the experimental electron density maps and then determined by nucleotide sequence analysis. Primary structure alignments reveal that Penicillium sp. beta-galactosidase belongs to family 35 of glycosyl hydrolases (GHF-35). This model is the first 3D structure for a member of GHF-35. Five distinct domains which comprise the structure are assembled in a way previously unobserved for beta-galactosidases. Superposition of this complex with other beta-galactosidase complexes from several hydrolase families allowed the identification of residue Glu200 as the proton donor and residue Glu299 as the nucleophile involved in catalysis. Penicillium sp. beta-galactosidase is a glycoprotein containing seven N-linked oligosaccharide chains and is the only structure of a glycosylated beta-galactosidase described to date.
About this StructureAbout this Structure
1TG7 is a Single protein structure of sequence from Penicillium sp.. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structures of beta-galactosidase from Penicillium sp. and its complex with galactose., Rojas AL, Nagem RA, Neustroev KN, Arand M, Adamska M, Eneyskaya EV, Kulminskaya AA, Garratt RC, Golubev AM, Polikarpov I, J Mol Biol. 2004 Nov 5;343(5):1281-92. PMID:15491613
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