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.

8gpb

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:8gpb.gif|left|200px]]
+
[[Image:8gpb.png|left|200px]]
<!--
<!--
Line 12: Line 12:
-
==Overview==
+
{{ABSTRACT_1900534}}
-
The crystal structures of activated R state glycogen phosphorylase a (GPa) and R and T state glycogen phosphorylase b (GPb) complexed with AMP have been solved at 2.9 A, 2.9 A and 2.2 A resolution, respectively. The structure of R state GPa is nearly identical to the structure of sulphate-activated R state GPb, except in the region of Ser14, where there is a covalently attached phosphate group in GPa and a non-covalently attached sulphate group in GPb. The contacts made by the N-terminal tail residues in R state GPa at the subunit interface of the functionally active dimer are similar to those observed previously for T state GPa. The quaternary and tertiary structural changes on the T to R transition allow these interactions to be relayed to the catalytic site in R state GPa. The transition from the T state GPb structure to the R state GPa structure results in a change in the N-terminal residues from a poorly ordered extended structure that makes intrasubunit contacts to an ordered coiled conformation that makes intersubunit contacts. The distance between Arg10, the first residue to be located from the N terminus, in R state GPa and T state GPb is 50 A. One of the important subunit-subunit interactions in the dimer molecule involves contacts between the helix alpha 2 and the cap' (residues 35' to 45' that form a loop between the 1st and 2nd alpha helices, alpha 1' and alpha 2' of the other subunit. The prime denotes residues from the other subunit). The interactions made by the N-terminal residues induce structural changes at the cap'/alpha 2 helix interface that lead to the creation of a high-affinity AMP site. The tertiary structural changes at the cap (shifts 1.2 to 2.1 A for residues 35 to 45) are partially compensated by the quaternary structural change so that the overall shifts in these residues after the combined tertiary and quaternary changes are between 0.5 and 1.3 A. AMP binds to R state GPb with at least 100-fold greater affinity and exhibits four additional hydrogen bonds, stronger ionic interactions and more extensive van der Waals' interactions with 116 A2 greater solvent accessible surface area buried compared with AMP bound to T state GPb.(ABSTRACT TRUNCATED AT 400 WORDS)
+
==About this Structure==
==About this Structure==
8GPB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. The following page contains interesting information on the relation of 8GPB with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb24_1.html Glycogen Phosphorylase]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8GPB OCA].
8GPB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. The following page contains interesting information on the relation of 8GPB with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb24_1.html Glycogen Phosphorylase]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8GPB OCA].
- 
-
==Reference==
 
-
Structural mechanism for glycogen phosphorylase control by phosphorylation and AMP., Barford D, Hu SH, Johnson LN, J Mol Biol. 1991 Mar 5;218(1):233-60. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1900534 1900534]
 
[[Category: Glycogen Phosphorylase]]
[[Category: Glycogen Phosphorylase]]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
Line 28: Line 24:
[[Category: Johnson, L N.]]
[[Category: Johnson, L N.]]
[[Category: Glycogen phosphorylase]]
[[Category: Glycogen phosphorylase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:49:21 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jun 26 18:31:44 2008''

Revision as of 15:31, 26 June 2008

Image:8gpb.png

Template:STRUCTURE 8gpb

STRUCTURAL MECHANISM FOR GLYCOGEN PHOSPHORYLASE CONTROL BY PHOSPHORYLATION AND AMP


Template:ABSTRACT 1900534

About this Structure

8GPB is a Single protein structure of sequence from Oryctolagus cuniculus. The following page contains interesting information on the relation of 8GPB with [Glycogen Phosphorylase]. Full crystallographic information is available from OCA.

Page seeded by OCA on Thu Jun 26 18:31:44 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/8gpb"
Personal tools