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1o99

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(New page: 200px<br /> <applet load="1o99" size="450" color="white" frame="true" align="right" spinBox="true" caption="1o99, resolution 2.65&Aring;" /> '''CRYSTAL STRUCTURE O...)
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==About this Structure==
==About this Structure==
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1O99 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Bacillus_stearothermophilus Bacillus stearothermophilus]] with MN, SO4 and 2PG as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1O99 OCA]].
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1O99 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=1O99 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]
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[[Category: Bacillus stearothermophilus]]
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[[Category: Geobacillus stearothermophilus]]
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[[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]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 21:26:43 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:01:32 2007''

Revision as of 11:56, 30 October 2007


1o99, resolution 2.65Å

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CRYSTAL STRUCTURE OF THE S62A MUTANT 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

1O99 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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