We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1qvb

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1qvb.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1qvb.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1qvb| PDB=1qvb | SCENE= }}
{{STRUCTURE_1qvb| PDB=1qvb | SCENE= }}
-
'''CRYSTAL STRUCTURE OF THE BETA-GLYCOSIDASE FROM THE HYPERTHERMOPHILE THERMOSPHAERA AGGREGANS'''
+
===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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10094493}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10094493 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10094493}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Thermostable]]
[[Category: Thermostable]]
[[Category: Tim-barrel]]
[[Category: Tim-barrel]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:44:35 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 04:13:18 2008''

Revision as of 01:13, 28 July 2008

Template:STRUCTURE 1qvb

CRYSTAL STRUCTURE OF THE BETA-GLYCOSIDASE FROM THE HYPERTHERMOPHILE THERMOSPHAERA AGGREGANS

Template:ABSTRACT PUBMED 10094493

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

Page seeded by OCA on Mon Jul 28 04:13:18 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools