1mum
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1mum.gif|left|200px]] | [[Image:1mum.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1mum", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | | | + | --> |
| - | | | + | {{STRUCTURE_1mum| PDB=1mum | SCENE= }} |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''Structure of the 2-Methylisocitrate Lyase (PrpB) from Escherichia coli''' | '''Structure of the 2-Methylisocitrate Lyase (PrpB) from Escherichia coli''' | ||
| Line 28: | Line 25: | ||
[[Category: Grimm, C.]] | [[Category: Grimm, C.]] | ||
[[Category: Reuter, K.]] | [[Category: Reuter, K.]] | ||
| - | [[Category: | + | [[Category: Lyase]] |
| - | [[Category: | + | [[Category: Methylcitrate cycle]] |
| - | [[Category: | + | [[Category: Methylisocitrate]] |
| - | [[Category: | + | [[Category: Prpb]] |
| - | [[Category: | + | [[Category: Tim-barrel]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:44:20 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 22:44, 2 May 2008
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. 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 Page seeded by OCA on Sat May 3 01:44:20 2008
