1ejj
From Proteopedia
(New page: 200px<br /><applet load="1ejj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ejj, resolution 1.90Å" /> '''CRYSTAL STRUCTURAL A...) |
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| - | [[Image:1ejj.gif|left|200px]]<br /><applet load="1ejj" size=" | + | [[Image:1ejj.gif|left|200px]]<br /><applet load="1ejj" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ejj, resolution 1.90Å" /> | caption="1ejj, resolution 1.90Å" /> | ||
'''CRYSTAL STRUCTURAL ANALYSIS OF PHOSPHOGLYCERATE MUTASE COCRYSTALLIZED WITH 3-PHOSPHOGLYCERATE'''<br /> | '''CRYSTAL STRUCTURAL ANALYSIS OF PHOSPHOGLYCERATE MUTASE COCRYSTALLIZED WITH 3-PHOSPHOGLYCERATE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Bacillus stearothermophilus phosphoglycerate mutase (PGM), which | + | Bacillus stearothermophilus phosphoglycerate mutase (PGM), which interconverts 2- and 3-phosphoglyceric acid (PGA), does not require 2,3-diphosphoglyceric acid for activity. However, this enzyme does have an absolute and specific requirement for Mn(2+) ions for catalysis. Here we report the crystal structure of this enzyme complexed with 3PGA and manganese ions to 1.9 A resolution; this is the first crystal structure of a diphosphoglycerate-independent PGM to be determined. This information, plus the location of the two bound Mn(2+) ions and the 3PGA have allowed formulation of a possible catalytic mechanism for this PGM. In this mechanism Mn(2+) ions facilitate the transfer of the substrate's phosphate group to Ser62 to form a phosphoserine intermediate. In the subsequent phosphotransferase part of the reaction, the phosphate group is transferred from Ser62 to the O2 or O3 positions of the reoriented glycerate to yield the PGA product. Site-directed mutagenesis studies were used to confirm our mechanism and the involvement of specific enzyme residues in Mn(2+) binding and catalysis. |
==About this Structure== | ==About this Structure== | ||
| - | 1EJJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus] with MN and 3PG as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Phosphoglycerate_mutase Phosphoglycerate mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.1 5.4.2.1] Full crystallographic information is available from [http:// | + | 1EJJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus] with <scene name='pdbligand=MN:'>MN</scene> and <scene name='pdbligand=3PG:'>3PG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Phosphoglycerate_mutase Phosphoglycerate mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.1 5.4.2.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EJJ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Chander, M.]] | [[Category: Chander, M.]] | ||
| - | [[Category: Jedrzejas, M | + | [[Category: Jedrzejas, M J.]] |
[[Category: Krishnasamy, G.]] | [[Category: Krishnasamy, G.]] | ||
[[Category: Setlow, P.]] | [[Category: Setlow, P.]] | ||
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[[Category: alpha/beta-type structure]] | [[Category: alpha/beta-type structure]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:28:25 2008'' |
Revision as of 10:28, 21 February 2008
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CRYSTAL STRUCTURAL ANALYSIS OF PHOSPHOGLYCERATE MUTASE COCRYSTALLIZED WITH 3-PHOSPHOGLYCERATE
Overview
Bacillus stearothermophilus phosphoglycerate mutase (PGM), which interconverts 2- and 3-phosphoglyceric acid (PGA), does not require 2,3-diphosphoglyceric acid for activity. However, this enzyme does have an absolute and specific requirement for Mn(2+) ions for catalysis. Here we report the crystal structure of this enzyme complexed with 3PGA and manganese ions to 1.9 A resolution; this is the first crystal structure of a diphosphoglycerate-independent PGM to be determined. This information, plus the location of the two bound Mn(2+) ions and the 3PGA have allowed formulation of a possible catalytic mechanism for this PGM. In this mechanism Mn(2+) ions facilitate the transfer of the substrate's phosphate group to Ser62 to form a phosphoserine intermediate. In the subsequent phosphotransferase part of the reaction, the phosphate group is transferred from Ser62 to the O2 or O3 positions of the reoriented glycerate to yield the PGA product. Site-directed mutagenesis studies were used to confirm our mechanism and the involvement of specific enzyme residues in Mn(2+) binding and catalysis.
About this Structure
1EJJ is a Single protein structure of sequence from Geobacillus stearothermophilus with and as ligands. Active as Phosphoglycerate mutase, with EC number 5.4.2.1 Full crystallographic information is available from OCA.
Reference
Structure and mechanism of action of a novel phosphoglycerate mutase from Bacillus stearothermophilus., Jedrzejas MJ, Chander M, Setlow P, Krishnasamy G, EMBO J. 2000 Apr 3;19(7):1419-31. PMID:10747010
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