This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


5gpb

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:5gpb.gif|left|200px]]
+
{{Seed}}
 +
[[Image:5gpb.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_5gpb| PDB=5gpb | SCENE= }}
{{STRUCTURE_5gpb| PDB=5gpb | SCENE= }}
-
'''COMPARISON OF THE BINDING OF GLUCOSE AND GLUCOSE-1-PHOSPHATE DERIVATIVES TO T-STATE GLYCOGEN PHOSPHORYLASE B'''
+
===COMPARISON OF THE BINDING OF GLUCOSE AND GLUCOSE-1-PHOSPHATE DERIVATIVES TO T-STATE GLYCOGEN PHOSPHORYLASE B===
-
==Overview==
+
<!--
-
The binding of T-state- and R-state-stabilizing ligands to the catalytic C site of T-state glycogen phosphorylase b has been investigated by crystallographic methods to study the interactions made and the conformational changes that occur at the C site. The compounds studied were alpha-D-glucose, 1, a T-state-stabilizing inhibitor of the enzyme, and the R-state-stabilizing phosphorylated ligands alpha-D-glucose 1-phosphate (2), 2-deoxy-2-fluoro-alpha-D-glucose 1-phosphate (3), and alpha-D-glucose 1-methylenephosphonate (4). The complexes have been refined, giving crystallographic R factors of less than 19%, for data between 8 and 2.3 A. Analysis of the refined structures shows that the glucosyl portions of the phosphorylated ligands bind in the same orientation as glucose and retain most of the interactions formed between glucose and the enzyme. However, the phosphates of the phosphorylated ligands adopt different conformations in each case; the stability of these conformations have been studied by using computational methods to rationalize the different binding modes. Binding of the phosphorylated ligands is accompanied by movement of C-site residues, most notably a shift of a loop out of the C site and toward the exterior of the protein. The C-site alterations do not include movement of Arg569, which has been observed in both the refined complex with 1-deoxy-D-gluco-heptulose 2-phosphate (5) [Johnson, L. N., et al (1990) J. Mol. Biol. 211, 645-661] and in the R-state enzyme [Barford, D. &amp; Johnson, L. N. (1989) Nature 340, 609-616]. Refinement of the ligand complexes has also led to the observation of additional electron density for residues 10-19 at the N-terminus which had not previously been localized in the native structure. The conformation of this stretch of residues is different from that observed in glycogen phosphorylase a.
+
The line below this paragraph, {{ABSTRACT_PUBMED_2125493}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 2125493 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_2125493}}
==About this Structure==
==About this Structure==
Line 25: Line 29:
[[Category: Martin, J L.]]
[[Category: Martin, J L.]]
[[Category: Glycogen phosphorylase]]
[[Category: Glycogen phosphorylase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:34:41 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 14:03:28 2008''

Revision as of 11:03, 3 July 2008

Image:5gpb.png

Template:STRUCTURE 5gpb

COMPARISON OF THE BINDING OF GLUCOSE AND GLUCOSE-1-PHOSPHATE DERIVATIVES TO T-STATE GLYCOGEN PHOSPHORYLASE B

Template:ABSTRACT PUBMED 2125493

About this Structure

5GPB is a Single protein structure. Full crystallographic information is available from OCA.

Reference

Comparison of the binding of glucose and glucose 1-phosphate derivatives to T-state glycogen phosphorylase b., Martin JL, Johnson LN, Withers SG, Biochemistry. 1990 Dec 4;29(48):10745-57. PMID:2125493

Page seeded by OCA on Thu Jul 3 14:03:28 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5gpb"
Personal tools