1qvb
From Proteopedia
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| - | [[Image:1qvb.jpg|left|200px]] | + | [[Image:1qvb.jpg|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF THE BETA-GLYCOSIDASE FROM THE HYPERTHERMOPHILE THERMOSPHAERA AGGREGANS''' | + | {{Structure |
| + | |PDB= 1qvb |SIZE=350|CAPTION= <scene name='initialview01'>1qvb</scene>, resolution 2.4Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF THE BETA-GLYCOSIDASE FROM THE HYPERTHERMOPHILE THERMOSPHAERA AGGREGANS''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1QVB is a [ | + | 1QVB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermosphaera_aggregans Thermosphaera aggregans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QVB OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure of the beta-glycosidase from the hyperthermophile Thermosphaera aggregans: insights into its activity and thermostability., Chi YI, Martinez-Cruz LA, Jancarik J, Swanson RV, Robertson DE, Kim SH, FEBS Lett. 1999 Feb 26;445(2-3):375-83. PMID:[http:// | + | Crystal structure of the beta-glycosidase from the hyperthermophile Thermosphaera aggregans: insights into its activity and thermostability., Chi YI, Martinez-Cruz LA, Jancarik J, Swanson RV, Robertson DE, Kim SH, FEBS Lett. 1999 Feb 26;445(2-3):375-83. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10094493 10094493] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Thermosphaera aggregans]] | [[Category: Thermosphaera aggregans]] | ||
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[[Category: tim-barrel]] | [[Category: tim-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 13:43:11 2008'' |
Revision as of 11:43, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE BETA-GLYCOSIDASE FROM THE HYPERTHERMOPHILE THERMOSPHAERA AGGREGANS
Overview
The glycosyl hydrolases are an important group of enzymes that are responsible for cleaving a range of biologically significant carbohydrate compounds. Structural information on these enzymes has provided useful information on their molecular basis for the functional variations, while the characterization of the structural features that account for the high thermostability of proteins is of great scientific and biotechnological interest. To these ends we have determined the crystal structure of the beta-glycosidase from a hyperthermophilic archeon Thermosphaera aggregans. The structure is a (beta/alpha)8 barrel (TIM-barrel), as seen in other glycosyl hydrolase family 1 members, and forms a tetramer. Inspection of the active site and the surrounding area reveals two catalytic glutamate residues consistent with the retaining mechanism and the surrounding polar and aromatic residues consistent with a monosaccharide binding site. Comparison of this structure with its mesophilic counterparts implicates a variety of structural features that could contribute to the thermostability. These include an increased number of surface ion pairs, an increased number of internal water molecules and a decreased surface area upon forming an oligomeric quaternary structure.
About this Structure
1QVB is a Single protein structure of sequence from Thermosphaera aggregans. Full crystallographic information is available from OCA.
Reference
Crystal structure of the beta-glycosidase from the hyperthermophile Thermosphaera aggregans: insights into its activity and thermostability., Chi YI, Martinez-Cruz LA, Jancarik J, Swanson RV, Robertson DE, Kim SH, FEBS Lett. 1999 Feb 26;445(2-3):375-83. PMID:10094493
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