1o98
From Proteopedia
(New page: 200px<br /> <applet load="1o98" size="450" color="white" frame="true" align="right" spinBox="true" caption="1o98, resolution 1.40Å" /> '''1.4A CRYSTAL STRUCT...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1O98 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/ | + | 1O98 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, SO4 and 2PG 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]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1O98 OCA]]. |
==Reference== | ==Reference== | ||
Insights into the catalytic mechanism of cofactor-independent phosphoglycerate mutase from X-ray crystallography, simulated dynamics and molecular modeling., Rigden DJ, Lamani E, Mello LV, Littlejohn JE, Jedrzejas MJ, J Mol Biol. 2003 May 9;328(4):909-20. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12729763 12729763] | Insights into the catalytic mechanism of cofactor-independent phosphoglycerate mutase from X-ray crystallography, simulated dynamics and molecular modeling., Rigden DJ, Lamani E, Mello LV, Littlejohn JE, Jedrzejas MJ, J Mol Biol. 2003 May 9;328(4):909-20. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12729763 12729763] | ||
| - | [[Category: | + | [[Category: Geobacillus stearothermophilus]] |
| + | [[Category: Phosphoglycerate mutase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Jedrzejas, M.J.]] | [[Category: Jedrzejas, M.J.]] | ||
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[[Category: isomerase]] | [[Category: isomerase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:02:06 2007'' |
Revision as of 11:57, 30 October 2007
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1.4A CRYSTAL STRUCTURE OF PHOSPHOGLYCERATE MUTASE FROM BACILLUS STEAROTHERMOPHILUS COMPLEXED WITH 2-PHOSPHOGLYCERATE
Overview
Phosphoglycerate mutases catalyze the isomerization of 2 and, 3-phosphoglycerates, and are essential for glucose metabolism in most, organisms. Here, we further characterize the, 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (iPGM) from, Bacillus stearothermophilus by determination of a high-resolution (1.4A), crystal structure of the wild-type enzyme and the crystal structure of its, S62A mutant. The mutant structure surprisingly showed the replacement of, one of the two catalytically essential manganese ions with a water, molecule, offering an additional possible explanation for its lack of, catalytic activity. Crystal structures invariably show substrate, phosphoglycerate to be entirely buried in a deep cleft between the two, iPGM domains. Flexibility analyses were ... [(full description)]
About this Structure
1O98 is a [Single protein] structure of sequence from [Geobacillus stearothermophilus] with MN, SO4 and 2PG as [ligands]. Active as [Phosphoglycerate mutase], with EC number [5.4.2.1]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Insights into the catalytic mechanism of cofactor-independent phosphoglycerate mutase from X-ray crystallography, simulated dynamics and molecular modeling., Rigden DJ, Lamani E, Mello LV, Littlejohn JE, Jedrzejas MJ, J Mol Biol. 2003 May 9;328(4):909-20. PMID:12729763
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