4ake: 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:4ake.gif|left|200px]]
{{Seed}}
[[Image:4ake.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_4ake|  PDB=4ake  |  SCENE=  }}  
{{STRUCTURE_4ake|  PDB=4ake  |  SCENE=  }}  


'''ADENYLATE KINASE'''
===ADENYLATE KINASE===




==Overview==
<!--
BACKGROUND: Adenylate kinases undergo large conformational changes during their catalytic cycle. Because these changes have been studied by comparison of structures from different species, which share approximately one-third of their residues, only rough descriptions have been possible to date. RESULTS: We have solved the structure of unligated adenylate kinase from Escherichia coli at 2.2 degree resolution and compared it with the high-resolution structure of the same enzyme ligated with an inhibitor mimicking both substrates, ATP and AMP. This comparison shows that, upon substrate binding, the enzyme increases its chain mobility in a region remote from the active center. As this region 'solidifies' again on substrate release, we propose that it serves as a 'counterweight' balancing the substrate binding energy. CONCLUSION: The comparison of two very different conformations of the same polypeptide chain revealed kinematic details of the catalytic cycle. Moreover, it indicated that there exists an energetic counterweight compensating the substrate binding energy required for specificity. This counterweight prevents the enzyme from dropping into a rate-reducing energy well along the reaction coordinate.
The line below this paragraph, {{ABSTRACT_PUBMED_8805521}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 8805521 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_8805521}}


==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Myokinase]]
[[Category: Myokinase]]
[[Category: Nucleoside monophosphate kinase]]
[[Category: Nucleoside monophosphate kinase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:20:39 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 13:27:55 2008''

Revision as of 10:27, 3 July 2008

File:4ake.png

Template:STRUCTURE 4ake

ADENYLATE KINASE

Template:ABSTRACT PUBMED 8805521

About this Structure

4AKE is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Adenylate kinase motions during catalysis: an energetic counterweight balancing substrate binding., Muller CW, Schlauderer GJ, Reinstein J, Schulz GE, Structure. 1996 Feb 15;4(2):147-56. PMID:8805521

Page seeded by OCA on Thu Jul 3 13:27:55 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=4ake&oldid=634375"