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.

1m80

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1m80.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1m80.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1m80| PDB=1m80 | SCENE= }}
{{STRUCTURE_1m80| PDB=1m80 | SCENE= }}
-
'''SUBSTRATE FREE FORM OF ARGININE KINASE'''
+
===SUBSTRATE FREE FORM OF ARGININE KINASE===
-
==Overview==
+
<!--
-
Arginine kinase (AK) is a member of the guanidino kinase family that plays an important role in buffering ATP concentration in cells with high and fluctuating energy demands. The AK specifically catalyzes the reversible phosphoryl transfer between ATP and arginine. We have determined the crystal structure of AK from the horseshoe crab (Limulus polyphemus) in its open (substrate-free) form. The final model has been refined at 2.35 A with a final R of 22.3% (R(free) = 23.7%). The structure of the open form is compared to the previously determined structure of the transition state analog complex in the closed form. Classically, the protein would be considered two domain, but dynamic domain (DynDom) analysis shows that most of the differences between the two structures can be considered as the motion between four rigid groups of nonsequential residues. ATP binds near a cluster of positively charged residues of a fixed dynamic domain. The other three dynamic domains close the active site with separate hinge rotations relative to the fixed domain. Several residues of key importance for the induced motion are conserved within the phosphagen kinase family, including creatine kinase. Substantial conformational changes are induced in different parts of the enzyme as intimate interactions are formed with both substrates. Thus, although induced fit occurs in a number of phosphoryl transfer enzymes, the conformational changes in phosphagen kinases appear to be more complicated than in prior examples.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12493833}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12493833 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12493833}}
==About this Structure==
==About this Structure==
Line 33: Line 37:
[[Category: Guanidino kina structure]]
[[Category: Guanidino kina structure]]
[[Category: Induced fit]]
[[Category: Induced fit]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:45:01 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 23:24:59 2008''

Revision as of 20:25, 2 July 2008

Image:1m80.png

Template:STRUCTURE 1m80

SUBSTRATE FREE FORM OF ARGININE KINASE

Template:ABSTRACT PUBMED 12493833

About this Structure

1M80 is a Single protein structure of sequence from Limulus polyphemus. Full crystallographic information is available from OCA.

Reference

Induced fit in guanidino kinases--comparison of substrate-free and transition state analog structures of arginine kinase., Yousef MS, Clark SA, Pruett PK, Somasundaram T, Ellington WR, Chapman MS, Protein Sci. 2003 Jan;12(1):103-11. PMID:12493833

Page seeded by OCA on Wed Jul 2 23:24:59 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1m80"
Personal tools