4ake

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
[[Image:4ake.gif|left|200px]]
[[Image:4ake.gif|left|200px]]
-
{{Structure
+
<!--
-
|PDB= 4ake |SIZE=350|CAPTION= <scene name='initialview01'>4ake</scene>, resolution 2.2&Aring;
+
The line below this paragraph, containing "STRUCTURE_4ake", creates the "Structure Box" on the page.
-
|SITE=
+
You may change the PDB parameter (which sets the PDB file loaded into the applet)
-
|LIGAND=
+
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenylate_kinase Adenylate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.3 2.7.4.3] </span>
+
or leave the SCENE parameter empty for the default display.
-
|GENE=
+
-->
-
|DOMAIN=
+
{{STRUCTURE_4ake| PDB=4ake | SCENE= }}
-
|RELATEDENTRY=
+
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ake FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ake OCA], [http://www.ebi.ac.uk/pdbsum/4ake PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=4ake RCSB]</span>
+
-
}}
+
'''ADENYLATE KINASE'''
'''ADENYLATE KINASE'''
Line 28: Line 25:
[[Category: Schlauderer, G J.]]
[[Category: Schlauderer, G J.]]
[[Category: Schulz, G E.]]
[[Category: Schulz, G E.]]
-
[[Category: atp:amp phosphotransferase]]
+
[[Category: Atp:amp phosphotransferase]]
-
[[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 Mon Mar 31 05:37:54 2008''
+

Revision as of 19:20, 4 May 2008

Image:4ake.gif

Template:STRUCTURE 4ake

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.

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 Sun May 4 22:20:39 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4ake"
Personal tools