1eqj
From Proteopedia
(New page: 200px<br /> <applet load="1eqj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1eqj, resolution 1.70Å" /> '''CRYSTAL STRUCTURE O...) |
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| - | [[Image:1eqj.gif|left|200px]]<br /> | + | [[Image:1eqj.gif|left|200px]]<br /><applet load="1eqj" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1eqj" size=" | + | |
caption="1eqj, resolution 1.70Å" /> | caption="1eqj, resolution 1.70Å" /> | ||
'''CRYSTAL STRUCTURE OF PHOSPHOGLYCERATE MUTASE FROM BACILLUS STEAROTHERMOPHILUS COMPLEXED WITH 2-PHOSPHOGLYCERATE'''<br /> | '''CRYSTAL STRUCTURE OF PHOSPHOGLYCERATE MUTASE FROM BACILLUS STEAROTHERMOPHILUS COMPLEXED WITH 2-PHOSPHOGLYCERATE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structure of the complex between the 2, 3-diphosphoglycerate-independent phosphoglycerate mutase (iPGM) from | + | The structure of the complex between the 2, 3-diphosphoglycerate-independent phosphoglycerate mutase (iPGM) from Bacillus stearothermophilus and its 3-phosphoglycerate substrate has recently been solved, and analysis of this structure allowed formulation of a mechanism for iPGM catalysis. In order to obtain further evidence for this mechanism, we have solved the structure of this iPGM complexed with 2-phosphoglycerate and two Mn(2+) ions at 1. 7-A resolution. The structure consists of two different domains connected by two loops and interacting through a network of hydrogen bonds. This structure is consistent with the proposed mechanism for iPGM catalysis, with the two main steps in catalysis being a phosphatase reaction removing the phosphate from 2- or 3-phosphoglycerate, generating an enzyme-bound phosphoserine intermediate, followed by a phosphotransferase reaction as the phosphate is transferred from the enzyme back to the glycerate moiety. The structure also allowed the assignment of the function of the two domains of the enzyme, one of which participates in the phosphatase reaction and formation of the phosphoserine enzyme intermediate, with the other involved in the phosphotransferase reaction regenerating phosphoglycerate. Significant structural similarity has also been found between the active site of the iPGM domain catalyzing the phosphatase reaction and Escherichia coli alkaline phosphatase. |
==About this Structure== | ==About this Structure== | ||
| - | 1EQJ 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 2PG as [http://en.wikipedia.org/wiki/ligands ligands]. The following page contains interesting information on the relation of 1EQJ with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb50_1.html The Glycolytic Enzymes]]. 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:// | + | 1EQJ 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=2PG:'>2PG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. The following page contains interesting information on the relation of 1EQJ with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb50_1.html The Glycolytic Enzymes]]. 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=1EQJ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: The Glycolytic Enzymes]] | [[Category: The Glycolytic Enzymes]] | ||
[[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 12:30:40 2008'' |
Revision as of 10:30, 21 February 2008
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CRYSTAL STRUCTURE OF PHOSPHOGLYCERATE MUTASE FROM BACILLUS STEAROTHERMOPHILUS COMPLEXED WITH 2-PHOSPHOGLYCERATE
Overview
The structure of the complex between the 2, 3-diphosphoglycerate-independent phosphoglycerate mutase (iPGM) from Bacillus stearothermophilus and its 3-phosphoglycerate substrate has recently been solved, and analysis of this structure allowed formulation of a mechanism for iPGM catalysis. In order to obtain further evidence for this mechanism, we have solved the structure of this iPGM complexed with 2-phosphoglycerate and two Mn(2+) ions at 1. 7-A resolution. The structure consists of two different domains connected by two loops and interacting through a network of hydrogen bonds. This structure is consistent with the proposed mechanism for iPGM catalysis, with the two main steps in catalysis being a phosphatase reaction removing the phosphate from 2- or 3-phosphoglycerate, generating an enzyme-bound phosphoserine intermediate, followed by a phosphotransferase reaction as the phosphate is transferred from the enzyme back to the glycerate moiety. The structure also allowed the assignment of the function of the two domains of the enzyme, one of which participates in the phosphatase reaction and formation of the phosphoserine enzyme intermediate, with the other involved in the phosphotransferase reaction regenerating phosphoglycerate. Significant structural similarity has also been found between the active site of the iPGM domain catalyzing the phosphatase reaction and Escherichia coli alkaline phosphatase.
About this Structure
1EQJ is a Single protein structure of sequence from Geobacillus stearothermophilus with and as ligands. The following page contains interesting information on the relation of 1EQJ with [The Glycolytic Enzymes]. Active as Phosphoglycerate mutase, with EC number 5.4.2.1 Full crystallographic information is available from OCA.
Reference
Mechanism of catalysis of the cofactor-independent phosphoglycerate mutase from Bacillus stearothermophilus. Crystal structure of the complex with 2-phosphoglycerate., Jedrzejas MJ, Chander M, Setlow P, Krishnasamy G, J Biol Chem. 2000 Jul 28;275(30):23146-53. PMID:10764795
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