1pfk

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1pfk.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1pfk.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1pfk| PDB=1pfk | SCENE= }}
{{STRUCTURE_1pfk| PDB=1pfk | SCENE= }}
-
'''CRYSTAL STRUCTURE OF THE COMPLEX OF PHOSPHOFRUCTOKINASE FROM ESCHERICHIA COLI WITH ITS REACTION PRODUCTS'''
+
===CRYSTAL STRUCTURE OF THE COMPLEX OF PHOSPHOFRUCTOKINASE FROM ESCHERICHIA COLI WITH ITS REACTION PRODUCTS===
-
==Overview==
+
<!--
-
The crystal structure of Escherichia coli phosphofructokinase complexed with its reaction products fructose 1,6-bisphosphate (Fru1,6P) and ADP/Mg2+, and the allosteric activator ADP/Mg2+, has been determined at 2.4 A resolution. The structure was solved by molecular replacement using the known structure of Bacillus stearothermophilus phosphofructokinase, and has been refined to a crystallographic R-factor of 0.165 for all data. The crystallization mixture contained the substrate fructose 6-phosphate, but the electron density maps showed clearly the presence of the product fructose 1,6-bisphosphate, presumably formed by the enzyme reaction with contaminating ATP. The crystal consists of tetrameric molecules with subunits in two different conformations despite their chemical identity. The magnesium ion in the "closed" subunit bridges the phosphate groups of the two products. In the "open" subunit, the products are about 1.5 A further apart, with the Mg2+ bound only to ADP. These two conformations probably represent two successive stages along the reaction pathway, in which the closure of the subunit is required to bring the substrates sufficiently close to react. This conformational change within the subunit is distinct from the quaternary structure change seen previously in the inactive T-state conformation. It is probably not involved in the co-operativity or allosteric control of the enzyme, since the co-operative product fructose 1,6-bisphosphate is not moved, nor are the subunit interfaces changed. The structure of the enzyme is similar to that of B. stearothermophilus phosphofructokinase, and confirms the location of the sites for the two reaction products (or substrates), and of the effector site binding the activator ADP/Mg2+. However, this structure gives a clearer picture of the active site, and of the interactions between the enzyme and its reaction products.
+
The line below this paragraph, {{ABSTRACT_PUBMED_2975709}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 2975709 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_2975709}}
==About this Structure==
==About this Structure==
Line 25: Line 29:
[[Category: Evans, P R.]]
[[Category: Evans, P R.]]
[[Category: Shirakihara, Y.]]
[[Category: Shirakihara, Y.]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:01:43 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 13:47:22 2008''

Revision as of 10:47, 29 July 2008

Image:1pfk.png


PDB ID 1pfk

Drag the structure with the mouse to rotate
1pfk, resolution 2.40Å ()
Ligands: , ,
Activity: 6-phosphofructokinase, with EC number 2.7.1.11
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF THE COMPLEX OF PHOSPHOFRUCTOKINASE FROM ESCHERICHIA COLI WITH ITS REACTION PRODUCTS

Template:ABSTRACT PUBMED 2975709

About this Structure

1PFK is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Crystal structure of the complex of phosphofructokinase from Escherichia coli with its reaction products., Shirakihara Y, Evans PR, J Mol Biol. 1988 Dec 20;204(4):973-94. PMID:2975709

Page seeded by OCA on Tue Jul 29 13:47:22 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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