1mum
From Proteopedia
(New page: 200px<br /><applet load="1mum" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mum, resolution 1.90Å" /> '''Structure of the 2-M...) |
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caption="1mum, resolution 1.90Å" /> | caption="1mum, resolution 1.90Å" /> | ||
'''Structure of the 2-Methylisocitrate Lyase (PrpB) from Escherichia coli'''<br /> | '''Structure of the 2-Methylisocitrate Lyase (PrpB) from Escherichia coli'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Following acetate, propionate is the second most abundant low molecular | + | Following acetate, propionate is the second most abundant low molecular mass carbon compound found in soil. Many microorganisms, including most, if not all fungi, as well as several aerobic bacteria, such as Escherichia coli and Salmonella enterica oxidize propionate via the methylcitrate cycle. The enzyme 2-methylisocitrate lyase (PrpB) from Escherichia coli catalysing the last step of this cycle, the cleavage of 2-methylisocitrate to pyruvate and succinate, was crystallised and its structure determined to a resolution of 1.9A. The enzyme, which strictly depends on Mg(2+) for catalysis, belongs to the isocitrate lyase protein family. A common feature of members of this enzyme family is the movement of a so-called "active site loop" from an open into a closed conformation upon substrate binding thus shielding the reactants from the surrounding solvent. Since in the presented structure, PrpB contains, apart from a Mg(2+), no ligand, the active site loop is found in an open conformation. This conformation, however, differs significantly from the open conformation present in the so far known structures of ligand-free isocitrate lyases. A possible impact of this observation with respect to the different responses of isocitrate lyases and PrpB upon treatment with the common inhibitor 3-bromopyruvate is discussed. Based on the structure of ligand-bound isocitrate lyase from Mycobacterium tuberculosis a model of the substrate-bound PrpB enzyme in its closed conformation was created which provides hints towards the substrate specificity of this enzyme. |
==About this Structure== | ==About this Structure== | ||
| - | 1MUM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with MG as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Methylisocitrate_lyase Methylisocitrate lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.3.30 4.1.3.30] Full crystallographic information is available from [http:// | + | 1MUM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Methylisocitrate_lyase Methylisocitrate lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.3.30 4.1.3.30] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MUM OCA]. |
==Reference== | ==Reference== | ||
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[[Category: tim-barrel]] | [[Category: tim-barrel]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:59:10 2008'' |
Revision as of 11:59, 21 February 2008
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Structure of the 2-Methylisocitrate Lyase (PrpB) from Escherichia coli
Overview
Following acetate, propionate is the second most abundant low molecular mass carbon compound found in soil. Many microorganisms, including most, if not all fungi, as well as several aerobic bacteria, such as Escherichia coli and Salmonella enterica oxidize propionate via the methylcitrate cycle. The enzyme 2-methylisocitrate lyase (PrpB) from Escherichia coli catalysing the last step of this cycle, the cleavage of 2-methylisocitrate to pyruvate and succinate, was crystallised and its structure determined to a resolution of 1.9A. The enzyme, which strictly depends on Mg(2+) for catalysis, belongs to the isocitrate lyase protein family. A common feature of members of this enzyme family is the movement of a so-called "active site loop" from an open into a closed conformation upon substrate binding thus shielding the reactants from the surrounding solvent. Since in the presented structure, PrpB contains, apart from a Mg(2+), no ligand, the active site loop is found in an open conformation. This conformation, however, differs significantly from the open conformation present in the so far known structures of ligand-free isocitrate lyases. A possible impact of this observation with respect to the different responses of isocitrate lyases and PrpB upon treatment with the common inhibitor 3-bromopyruvate is discussed. Based on the structure of ligand-bound isocitrate lyase from Mycobacterium tuberculosis a model of the substrate-bound PrpB enzyme in its closed conformation was created which provides hints towards the substrate specificity of this enzyme.
About this Structure
1MUM is a Single protein structure of sequence from Escherichia coli with as ligand. Active as Methylisocitrate lyase, with EC number 4.1.3.30 Full crystallographic information is available from OCA.
Reference
Crystal structure of 2-methylisocitrate lyase (PrpB) from Escherichia coli and modelling of its ligand bound active centre., Grimm C, Evers A, Brock M, Maerker C, Klebe G, Buckel W, Reuter K, J Mol Biol. 2003 May 2;328(3):609-21. PMID:12706720
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