1qb4: Difference between revisions

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[[Image:1qb4.gif|left|200px]]
{{Seed}}
[[Image:1qb4.png|left|200px]]


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{{STRUCTURE_1qb4|  PDB=1qb4  |  SCENE=  }}  
{{STRUCTURE_1qb4|  PDB=1qb4  |  SCENE=  }}  


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




==Overview==
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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.
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{{ABSTRACT_PUBMED_10481043}}


==About this Structure==
==About this Structure==
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[[Category: Yoshinaga, T.]]
[[Category: Yoshinaga, T.]]
[[Category: Alpha beta barrel]]
[[Category: Alpha beta barrel]]
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