1a3x

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1a3x.gif|left|200px]]<br /><applet load="1a3x" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1a3x.gif|left|200px]]
-
caption="1a3x, resolution 3.0&Aring;" />
+
 
-
'''PYRUVATE KINASE FROM SACCHAROMYCES CEREVISIAE COMPLEXED WITH PG, MN2+ AND K+'''<br />
+
{{Structure
 +
|PDB= 1a3x |SIZE=350|CAPTION= <scene name='initialview01'>1a3x</scene>, resolution 3.0&Aring;
 +
|SITE=
 +
|LIGAND= <scene name='pdbligand=PGA:2-PHOSPHOGLYCOLIC+ACID'>PGA</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> and <scene name='pdbligand=K:POTASSIUM ION'>K</scene>
 +
|ACTIVITY= [http://en.wikipedia.org/wiki/Pyruvate_kinase Pyruvate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.40 2.7.1.40]
 +
|GENE=
 +
}}
 +
 
 +
'''PYRUVATE KINASE FROM SACCHAROMYCES CEREVISIAE COMPLEXED WITH PG, MN2+ AND K+'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
1A3X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=PGA:'>PGA</scene>, <scene name='pdbligand=MN:'>MN</scene> and <scene name='pdbligand=K:'>K</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Pyruvate_kinase Pyruvate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.40 2.7.1.40] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A3X OCA].
+
1A3X is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A3X OCA].
==Reference==
==Reference==
-
The allosteric regulation of pyruvate kinase by fructose-1,6-bisphosphate., Jurica MS, Mesecar A, Heath PJ, Shi W, Nowak T, Stoddard BL, Structure. 1998 Feb 15;6(2):195-210. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9519410 9519410]
+
The allosteric regulation of pyruvate kinase by fructose-1,6-bisphosphate., Jurica MS, Mesecar A, Heath PJ, Shi W, Nowak T, Stoddard BL, Structure. 1998 Feb 15;6(2):195-210. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9519410 9519410]
[[Category: Pyruvate kinase]]
[[Category: Pyruvate kinase]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
Line 27: Line 36:
[[Category: tranferase]]
[[Category: tranferase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:40:34 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:52:34 2008''

Revision as of 07:52, 20 March 2008

Image:1a3x.gif


PDB ID 1a3x

Drag the structure with the mouse to rotate
, resolution 3.0Å
Ligands: , and
Activity: Pyruvate kinase, with EC number 2.7.1.40
Coordinates: save as pdb, mmCIF, xml



PYRUVATE KINASE FROM SACCHAROMYCES CEREVISIAE COMPLEXED WITH PG, MN2+ AND K+


Overview

BACKGROUND: Yeast pyruvate kinase (PK) catalyzes the final step in glycolysis. The enzyme therefore represents an important control point and is allosterically activated by fructose-1,6-bisphosphate (FBP). In mammals the enzyme is found as four different isozymes with different regulatory properties: two of these isozymes are produced by alternate splicing. The allosteric regulation of PK is directly related to proliferation of certain cell types, as demonstrated by the expression of an allosterically regulated isozyme in tumor cells. A model for the allosteric transition from the inactive (T) state to the active (R) state has been proposed previously, but until now the FBP-binding site had not been identified. RESULTS: We report here the structures of PK from yeast complexed with a substrate analog and catalytic metal ions in the presence and absence of bound FBP. The allosteric site is located 40 A from the active site and is entirely located in the enzyme regulatory (C) domain. A phosphate-binding site for the allosteric activator is created by residues encoded by a region of the gene corresponding to the alternately spliced exon of mammalian isozymes. FBP activation appears to induce several conformational changes among active-site sidechains through a mechanism that is most likely to involve significant domain motions, as previously hypothesized. CONCLUSIONS: The structure and location of the allosteric activator site agrees with the pattern of alternate genetic splicing of the PK gene in multicellular eukaryotes that distinguishes between a non-regulated isozyme and the regulated fetal isozymes. The conformational differences observed between the active sites of inactive and fully active PK enzymes is in agreement with the recently determined thermodynamic mechanism of allosteric activation through a 'metal relay' that increases the affinity of the enzyme for its natural phosphoenolpyruvate substrate.

About this Structure

1A3X is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

The allosteric regulation of pyruvate kinase by fructose-1,6-bisphosphate., Jurica MS, Mesecar A, Heath PJ, Shi W, Nowak T, Stoddard BL, Structure. 1998 Feb 15;6(2):195-210. PMID:9519410

Page seeded by OCA on Thu Mar 20 09:52:34 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1a3x"
Personal tools