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.


1fpb

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1fpb.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1fpb.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1fpb| PDB=1fpb | SCENE= }}
{{STRUCTURE_1fpb| PDB=1fpb | SCENE= }}
-
'''CRYSTAL STRUCTURE OF THE NEUTRAL FORM OF FRUCTOSE 1,6-BISPHOSPHATASE COMPLEXED WITH REGULATORY INHIBITOR FRUCTOSE 2,6-BISPHOSPHATE AT 2.6-ANGSTROMS RESOLUTION'''
+
===CRYSTAL STRUCTURE OF THE NEUTRAL FORM OF FRUCTOSE 1,6-BISPHOSPHATASE COMPLEXED WITH REGULATORY INHIBITOR FRUCTOSE 2,6-BISPHOSPHATE AT 2.6-ANGSTROMS RESOLUTION===
-
==Overview==
+
<!--
-
The three-dimensional structure of the complex between fructose 1,6-bisphosphatase (EC 3.1.3.11) and the physiological inhibitor beta-D-fructose 2,6-bisphosphate (Fru-2,6-P2), an analogue of the substrate (fructose 1,6-bisphosphate), has been refined at 2.6-A resolution to a residual error (R) factor of 0.171. The rms deviations are 0.012 A and 2.88 degrees from ideal geometries of bond lengths and angles, respectively. The Fru-2,6-P2 occupies the active sites of both polypeptides C1 and C2 in the crystallographic asymmetric unit in the space group P3(2)21. The furanose and 6-phosphate of Fru-2,6-P2 are located at the fructose 6-phosphate site established earlier, and the 2-phosphate binds to the OH of Ser-124, the NH3+ of Lys-274, and the backbone NH of Gly-122 and Ser-123. Backbone displacements of 1 A occur for residues from Asp-121 to Asn-125. Model building of substrate alpha-D-Fru-1,6-P2 based on the binding structure of Fru-2,6-P2 in the active site shows interactions of the 1-phosphate with the backbone NH of Ser-123 and Ser-124. In the AMP sites, density peaks attributed to Fru-2,6-P2 are seen in C1 (and C4) but not in C2 (and C3). This minor binding of Fru-2,6-P2 to AMP sites partially explains the synergistic interaction between AMP and Fru-2,6-P2 and the protection of the AMP site from acetylation in the presence of Fru-2,6-P2. In the synergistic interaction between AMP and Fru-2,6-P2, inhibition of catalytic metal binding by the presence of Fru-2,6-P2 at the active site, and propagation of structural changes over some 28 A along beta-strand B3 from residues 121 to 125 in the active site to Lys-112 and Tyr-113 in the AMP site, as well as movement of helices across the interdimeric interfaces, may affect AMP binding and the subsequent R-to-T transition. In addition, occupancy of Fru-2,6-P2 at the AMP sites of C1 and C4 may favor binding of AMP to the remaining unoccupied AMP sites and thus promote the accompanying quaternary conformational changes.
+
The line below this paragraph, {{ABSTRACT_PUBMED_1312721}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 1312721 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_1312721}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Lipscomb, W N.]]
[[Category: Lipscomb, W N.]]
[[Category: Zhang, Y.]]
[[Category: Zhang, Y.]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:36:23 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 03:43:42 2008''

Revision as of 00:43, 1 July 2008

Image:1fpb.png

Template:STRUCTURE 1fpb

CRYSTAL STRUCTURE OF THE NEUTRAL FORM OF FRUCTOSE 1,6-BISPHOSPHATASE COMPLEXED WITH REGULATORY INHIBITOR FRUCTOSE 2,6-BISPHOSPHATE AT 2.6-ANGSTROMS RESOLUTION

Template:ABSTRACT PUBMED 1312721

About this Structure

1FPB is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.

Reference

Crystal structure of the neutral form of fructose 1,6-bisphosphatase complexed with regulatory inhibitor fructose 2,6-bisphosphate at 2.6-A resolution., Liang JY, Huang S, Zhang Y, Ke H, Lipscomb WN, Proc Natl Acad Sci U S A. 1992 Mar 15;89(6):2404-8. PMID:1312721

Page seeded by OCA on Tue Jul 1 03:43:42 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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