2hk3
From Proteopedia
(New page: 200px<br /><applet load="2hk3" size="350" color="white" frame="true" align="right" spinBox="true" caption="2hk3, resolution 2.300Å" /> '''Crystal structure o...) |
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==Overview== | ==Overview== | ||
| - | Mevalonate diphosphate decarboxylase (MDD) catalyzes the ATP-dependent | + | Mevalonate diphosphate decarboxylase (MDD) catalyzes the ATP-dependent decarboxylation of mevalonate 5-diphosphate (MDP) to form isopentenyl pyrophosphate, a ubiquitous precursor for isoprenoid biosynthesis. MDD is a poorly understood component of this important metabolic pathway. Complementation of a temperature-sensitive yeast mutant by the putative mdd genes of Trypanosoma brucei and Staphylococcus aureus provides proof-of-function. Crystal structures of MDD from T. brucei (TbMDD, at 1.8 A resolution) and S. aureus (SaMDD, in two distinct crystal forms, each diffracting to 2.3 A resolution) have been determined. Gel-filtration chromatography and analytical ultracentrifugation experiments indicate that TbMDD is predominantly monomeric in solution while SaMDD is dimeric. The new crystal structures and comparison with that of the yeast Saccharomyces cerevisiae enzyme (ScMDD) reveal the structural basis for this variance in quaternary structure. The presence of an ordered sulfate in the structure of TbMDD reveals for the first time details of a ligand binding in the MDD active site and, in conjunction with well-ordered water molecules, comparisons with the related enzyme mevalonate kinase, structural and biochemical data derived on ScMDD and SaMDD, allows us to model a ternary complex with MDP and ATP. This model facilitates discussion of the molecular determinants of substrate recognition and contributions made by specific residues to the enzyme mechanism. |
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
| - | Crystal | + | Crystal structures of Trypanosoma brucei and Staphylococcus aureus mevalonate diphosphate decarboxylase inform on the determinants of specificity and reactivity., Byres E, Alphey MS, Smith TK, Hunter WN, J Mol Biol. 2007 Aug 10;371(2):540-53. Epub 2007 Jun 4. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17583736 17583736] |
[[Category: Diphosphomevalonate decarboxylase]] | [[Category: Diphosphomevalonate decarboxylase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Staphylococcus aureus]] | [[Category: Staphylococcus aureus]] | ||
[[Category: Byres, E.]] | [[Category: Byres, E.]] | ||
| - | [[Category: Hunter, W | + | [[Category: Hunter, W N.]] |
[[Category: decarboxylase]] | [[Category: decarboxylase]] | ||
[[Category: diphosphomevalonate decarboxylase]] | [[Category: diphosphomevalonate decarboxylase]] | ||
[[Category: mevalonate diphosphate decarboxylase]] | [[Category: mevalonate diphosphate decarboxylase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:42:44 2008'' |
Revision as of 15:42, 21 February 2008
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Crystal structure of mevalonate diphosphate decarboxylase from Staphylococcus aureus (orthorhombic form)
Overview
Mevalonate diphosphate decarboxylase (MDD) catalyzes the ATP-dependent decarboxylation of mevalonate 5-diphosphate (MDP) to form isopentenyl pyrophosphate, a ubiquitous precursor for isoprenoid biosynthesis. MDD is a poorly understood component of this important metabolic pathway. Complementation of a temperature-sensitive yeast mutant by the putative mdd genes of Trypanosoma brucei and Staphylococcus aureus provides proof-of-function. Crystal structures of MDD from T. brucei (TbMDD, at 1.8 A resolution) and S. aureus (SaMDD, in two distinct crystal forms, each diffracting to 2.3 A resolution) have been determined. Gel-filtration chromatography and analytical ultracentrifugation experiments indicate that TbMDD is predominantly monomeric in solution while SaMDD is dimeric. The new crystal structures and comparison with that of the yeast Saccharomyces cerevisiae enzyme (ScMDD) reveal the structural basis for this variance in quaternary structure. The presence of an ordered sulfate in the structure of TbMDD reveals for the first time details of a ligand binding in the MDD active site and, in conjunction with well-ordered water molecules, comparisons with the related enzyme mevalonate kinase, structural and biochemical data derived on ScMDD and SaMDD, allows us to model a ternary complex with MDP and ATP. This model facilitates discussion of the molecular determinants of substrate recognition and contributions made by specific residues to the enzyme mechanism.
About this Structure
2HK3 is a Single protein structure of sequence from Staphylococcus aureus. Active as Diphosphomevalonate decarboxylase, with EC number 4.1.1.33 Full crystallographic information is available from OCA.
Reference
Crystal structures of Trypanosoma brucei and Staphylococcus aureus mevalonate diphosphate decarboxylase inform on the determinants of specificity and reactivity., Byres E, Alphey MS, Smith TK, Hunter WN, J Mol Biol. 2007 Aug 10;371(2):540-53. Epub 2007 Jun 4. PMID:17583736
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