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.


1xfb

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1xfb.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1xfb.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1xfb| PDB=1xfb | SCENE= }}
{{STRUCTURE_1xfb| PDB=1xfb | SCENE= }}
-
'''Human Brain Fructose 1,6-(bis)phosphate Aldolase (C isozyme)'''
+
===Human Brain Fructose 1,6-(bis)phosphate Aldolase (C isozyme)===
-
==Overview==
+
<!--
-
Fructose-1,6-(bis)phosphate aldolase is a ubiquitous enzyme that catalyzes the reversible aldol cleavage of fructose-1,6-(bis)phosphate and fructose 1-phosphate to dihydroxyacetone phosphate and either glyceral-dehyde-3-phosphate or glyceraldehyde, respectively. Vertebrate aldolases exist as three isozymes with different tissue distributions and kinetics: aldolase A (muscle and red blood cell), aldolase B (liver, kidney, and small intestine), and aldolase C (brain and neuronal tissue). The structures of human aldolases A and B are known and herein we report the first structure of the human aldolase C, solved by X-ray crystallography at 3.0 A resolution. Structural differences between the isozymes were expected to account for isozyme-specific activity. However, the structures of isozymes A, B, and C are the same in their overall fold and active site structure. The subtle changes observed in active site residues Arg42, Lys146, and Arg303 are insufficient to completely account for the tissue-specific isozymic differences. Consequently, the structural analysis has been extended to the isozyme-specific residues (ISRs), those residues conserved among paralogs. A complete analysis of the ISRs in the context of this structure demonstrates that in several cases an amino acid residue that is conserved among aldolase C orthologs prevents an interaction that occurs in paralogs. In addition, the structure confirms the clustering of ISRs into discrete patches on the surface and reveals the existence in aldolase C of a patch of electronegative residues localized near the C terminus. Together, these structural changes highlight the differences required for the tissue and kinetic specificity among aldolase isozymes.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15537755}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15537755 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15537755}}
==About this Structure==
==About this Structure==
Line 35: Line 39:
[[Category: Structural enzymology]]
[[Category: Structural enzymology]]
[[Category: Structure/function]]
[[Category: Structure/function]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 14:57:16 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 00:34:18 2008''

Revision as of 21:34, 28 July 2008

Image:1xfb.png

Template:STRUCTURE 1xfb

Human Brain Fructose 1,6-(bis)phosphate Aldolase (C isozyme)

Template:ABSTRACT PUBMED 15537755

About this Structure

1XFB is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structure of human brain fructose 1,6-(bis)phosphate aldolase: linking isozyme structure with function., Arakaki TL, Pezza JA, Cronin MA, Hopkins CE, Zimmer DB, Tolan DR, Allen KN, Protein Sci. 2004 Dec;13(12):3077-84. Epub 2004 Nov 10. PMID:15537755

Page seeded by OCA on Tue Jul 29 00:34:18 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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