1qb4: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
New page: left|200px<br /><applet load="1qb4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qb4, resolution 2.6Å" /> '''CRYSTAL STRUCTURE OF ...
 
No edit summary
Line 1: Line 1:
[[Image:1qb4.gif|left|200px]]<br /><applet load="1qb4" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1qb4.gif|left|200px]]<br /><applet load="1qb4" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1qb4, resolution 2.6&Aring;" />
caption="1qb4, resolution 2.6&Aring;" />
'''CRYSTAL STRUCTURE OF MN(2+)-BOUND PHOSPHOENOLPYRUVATE CARBOXYLASE'''<br />
'''CRYSTAL STRUCTURE OF MN(2+)-BOUND PHOSPHOENOLPYRUVATE CARBOXYLASE'''<br />


==Overview==
==Overview==
We have determined the crystal structure of Mn2+-bound Escherichia coli, phosphoenolpyruvate carboxylase (PEPC) using X-ray diffraction at 2.6 A, resolution, and specified the location of enzyme-bound Mn2+, which is, essential for catalytic activity. The electron density map reveals that, Mn2+ is bound to the side chain oxygens of Glu-506 and Asp-543, and, located at the top of the alpha/beta barrel in PEPC. The coordination, sphere of Mn2+ observed in E. coli PEPC is similar to that of Mn2+ found, in the pyruvate kinase structure. The model study of Mn2+-bound PEPC, complexed with phosphoenolpyruvate (PEP) reveals that the side chains of, Arg-396, Arg-581 and Arg-713 could interact with PEP.
We have determined the crystal structure of Mn2+-bound Escherichia coli phosphoenolpyruvate carboxylase (PEPC) using X-ray diffraction at 2.6 A resolution, and specified the location of enzyme-bound Mn2+, which is essential for catalytic activity. The electron density map reveals that Mn2+ is bound to the side chain oxygens of Glu-506 and Asp-543, and located at the top of the alpha/beta barrel in PEPC. The coordination sphere of Mn2+ observed in E. coli PEPC is similar to that of Mn2+ found in the pyruvate kinase structure. The model study of Mn2+-bound PEPC complexed with phosphoenolpyruvate (PEP) reveals that the side chains of Arg-396, Arg-581 and Arg-713 could interact with PEP.


==About this Structure==
==About this Structure==
1QB4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with MN and ASP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Phosphoenolpyruvate_carboxylase Phosphoenolpyruvate carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.31 4.1.1.31] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QB4 OCA].  
1QB4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=MN:'>MN</scene> and <scene name='pdbligand=ASP:'>ASP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Phosphoenolpyruvate_carboxylase Phosphoenolpyruvate carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.31 4.1.1.31] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QB4 OCA].  


==Reference==
==Reference==
Line 25: Line 25:
[[Category: alpha beta barrel]]
[[Category: alpha beta barrel]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:32:57 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:37:46 2008''

Revision as of 15:37, 21 February 2008

File:1qb4.gif


1qb4, resolution 2.6Å

Drag the structure with the mouse to rotate

CRYSTAL STRUCTURE OF MN(2+)-BOUND PHOSPHOENOLPYRUVATE CARBOXYLASE

OverviewOverview

We have determined the crystal structure of Mn2+-bound Escherichia coli phosphoenolpyruvate carboxylase (PEPC) using X-ray diffraction at 2.6 A resolution, and specified the location of enzyme-bound Mn2+, which is essential for catalytic activity. The electron density map reveals that Mn2+ is bound to the side chain oxygens of Glu-506 and Asp-543, and located at the top of the alpha/beta barrel in PEPC. The coordination sphere of Mn2+ observed in E. coli PEPC is similar to that of Mn2+ found in the pyruvate kinase structure. The model study of Mn2+-bound PEPC complexed with phosphoenolpyruvate (PEP) reveals that the side chains of Arg-396, Arg-581 and Arg-713 could interact with PEP.

About this StructureAbout this Structure

1QB4 is a Single protein structure of sequence from Escherichia coli with and as ligands. Active as Phosphoenolpyruvate carboxylase, with EC number 4.1.1.31 Full crystallographic information is available from OCA.

ReferenceReference

Plausible phosphoenolpyruvate binding site revealed by 2.6 A structure of Mn2+-bound phosphoenolpyruvate carboxylase from Escherichia coli., Matsumura H, Terada M, Shirakata S, Inoue T, Yoshinaga T, Izui K, Kai Y, FEBS Lett. 1999 Sep 17;458(2):93-6. PMID:10481043

Page seeded by OCA on Thu Feb 21 14:37:46 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA