2btm: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
Line 1: Line 1:
[[Image:2btm.gif|left|200px]]
{{Seed}}
[[Image:2btm.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2btm|  PDB=2btm  |  SCENE=  }}  
{{STRUCTURE_2btm|  PDB=2btm  |  SCENE=  }}  


'''DOES THE HIS12-LYS13 PAIR PLAY A ROLE IN THE ADAPTATION OF THERMOPHILIC TIMS TO HIGH TEMPERATURES?'''
===DOES THE HIS12-LYS13 PAIR PLAY A ROLE IN THE ADAPTATION OF THERMOPHILIC TIMS TO HIGH TEMPERATURES?===




==Overview==
<!--
The thermophilic triose-phosphate isomerases (TIMs) of Bacillus stearothermophilus (bTIM) and Thermotoga maritima (tTIM) have been found to possess a His12-Lys13 pair instead of the Asn12-Gly13 pair normally present in mesophilic TIMs. His12 in bTIM was proposed to prevent deamidation at high temperature, while the precise role of Lys13 is unknown. To investigate the role of the His12 and Lys13 pair in the enzyme's thermoadaptation, we reintroduced the "mesophilic residues" Asn and Gly into both thermophilic TIMs. Neither double mutant displayed diminished structural stability, but the bTIM double mutant showed drastically reduced catalytic activity. No similar behavior was observed with the tTIM double mutant, suggesting that the presence of the His12 and Lys13 cannot be systematically correlated to thermoadaptation in TIMs. We determined the crystal structure of the bTIM double mutant complexed with 2-phosphoglycolate to 2.4-A resolution. A molecular dynamics simulation showed that upon substitution of Lys13 to Gly an increase of the flexibility of loop 1 is observed, causing an incorrect orientation of the catalytic Lys10. This suggests that Lys13 in bTIM plays a crucial role in the functional adaptation of this enzyme to high temperature. Analysis of bTIM single mutants supports this assumption.
The line below this paragraph, {{ABSTRACT_PUBMED_10383424}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 10383424 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_10383424}}


==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Glycolysis]]
[[Category: Glycolysis]]
[[Category: Thermophilic triose-phosphate]]
[[Category: Thermophilic triose-phosphate]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 20:46:49 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 03:53:23 2008''

Revision as of 00:53, 28 July 2008

File:2btm.png

Template:STRUCTURE 2btm

DOES THE HIS12-LYS13 PAIR PLAY A ROLE IN THE ADAPTATION OF THERMOPHILIC TIMS TO HIGH TEMPERATURES?

Template:ABSTRACT PUBMED 10383424

About this Structure

2BTM is a Single protein structure of sequence from Geobacillus stearothermophilus. Full crystallographic information is available from OCA.

Reference

Lys13 plays a crucial role in the functional adaptation of the thermophilic triose-phosphate isomerase from Bacillus stearothermophilus to high temperatures., Alvarez M, Wouters J, Maes D, Mainfroid V, Rentier-Delrue F, Wyns L, Depiereux E, Martial JA, J Biol Chem. 1999 Jul 2;274(27):19181-7. PMID:10383424

Page seeded by OCA on Mon Jul 28 03:53:23 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=2btm&oldid=679816"