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1qb4

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[[Image:1qb4.gif|left|200px]]
[[Image:1qb4.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1qb4 |SIZE=350|CAPTION= <scene name='initialview01'>1qb4</scene>, resolution 2.6&Aring;
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The line below this paragraph, containing "STRUCTURE_1qb4", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=ASP:ASPARTIC+ACID'>ASP</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= K12 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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-->
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|DOMAIN=
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{{STRUCTURE_1qb4| PDB=1qb4 | SCENE= }}
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|RELATEDENTRY=[[1fiy|1FIY]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qb4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qb4 OCA], [http://www.ebi.ac.uk/pdbsum/1qb4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qb4 RCSB]</span>
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}}
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'''CRYSTAL STRUCTURE OF MN(2+)-BOUND PHOSPHOENOLPYRUVATE CARBOXYLASE'''
'''CRYSTAL STRUCTURE OF MN(2+)-BOUND PHOSPHOENOLPYRUVATE CARBOXYLASE'''
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[[Category: Terada, M.]]
[[Category: Terada, M.]]
[[Category: Yoshinaga, T.]]
[[Category: Yoshinaga, T.]]
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[[Category: alpha beta barrel]]
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[[Category: Alpha beta barrel]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:05:22 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:11:17 2008''
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Revision as of 03:05, 3 May 2008

Image:1qb4.gif

Template:STRUCTURE 1qb4

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


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.

About this Structure

1QB4 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

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 Sat May 3 06:05:22 2008

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