1gow: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
Line 1: Line 1:
[[Image:1gow.gif|left|200px]]
{{Seed}}
[[Image:1gow.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1gow|  PDB=1gow  |  SCENE=  }}  
{{STRUCTURE_1gow|  PDB=1gow  |  SCENE=  }}  


'''BETA-GLYCOSIDASE FROM SULFOLOBUS SOLFATARICUS'''
===BETA-GLYCOSIDASE FROM SULFOLOBUS SOLFATARICUS===




==Overview==
<!--
Enzymes from hyperthermophilic organisms must operate at temperatures which rapidly denature proteins from mesophiles. The structural basis of this thermostability is still poorly understood. Towards a further understanding of hyperthermostability, we have determined the crystal structure of the beta-glycosidase (clan GH-1A, family 1) from the hyperthermophilic archaeon Sulfolobus solfataricus at 2.6 A resolution. The enzyme is a tetramer with subunit molecular mass at 60 kDa, and crystallises with half of the tetramer in the asymmetric unit. The structure is a (betaalpha)8 barrel, but with substantial elaborations between the beta-strands and alpha-helices in each repeat. The active site occurs at the centre of the top face of the barrel and is connected to the surface by a radial channel which becomes a blind-ended tunnel in the tetramer, and probably acts as the binding site for extended oligosaccharide substrates. Analysis of the structure reveals two features which differ significantly from mesophile proteins; (1) an unusually large proportion of surface ion-pairs involved in networks that cross-link sequentially separate structures on the protein surface, and (2) an unusually large number of solvent molecules buried in hydrophilic cavities between sequentially separate structures in the protein core. These factors suggest a model for hyperthermostability via resilience rather than rigidity.
The line below this paragraph, {{ABSTRACT_PUBMED_9299327}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 9299327 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_9299327}}


==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Beta-glycosidase]]
[[Category: Beta-glycosidase]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:50:14 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 05:37:21 2008''

Revision as of 02:37, 1 July 2008

File:1gow.png

Template:STRUCTURE 1gow

BETA-GLYCOSIDASE FROM SULFOLOBUS SOLFATARICUS

Template:ABSTRACT PUBMED 9299327

About this Structure

1GOW is a Single protein structure of sequence from Sulfolobus solfataricus. Full crystallographic information is available from OCA.

Reference

Crystal structure of the beta-glycosidase from the hyperthermophilic archeon Sulfolobus solfataricus: resilience as a key factor in thermostability., Aguilar CF, Sanderson I, Moracci M, Ciaramella M, Nucci R, Rossi M, Pearl LH, J Mol Biol. 1997 Sep 5;271(5):789-802. PMID:9299327

Page seeded by OCA on Tue Jul 1 05:37:21 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1gow&oldid=603212"