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| {{STRUCTURE_2dft| PDB=2dft | SCENE= }} | | {{STRUCTURE_2dft| PDB=2dft | SCENE= }} |
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| '''Structure of shikimate kinase from Mycobacterium tuberculosis complexed with ADP and Mg at 2.8 angstrons of resolution'''
| | ===Structure of shikimate kinase from Mycobacterium tuberculosis complexed with ADP and Mg at 2.8 angstrons of resolution=== |
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| ==Overview==
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| Bacteria, fungi and plants can convert carbohydrate and phosphoenolpyruvate into chorismate, which is the precursor of various aromatic compounds. The seven enzymes of the shikimate pathway are responsible for this conversion. Shikimate kinase (SK) is the fifth enzyme in this pathway and converts shikimate to shikimate-3-phosphate. In this work, the conformational changes that occur on binding of shikimate, magnesium and chloride ions to SK from Mycobacterium tuberculosis (MtSK) are described. It was observed that both ions and shikimate influence the conformation of residues of the active site of MtSK. Magnesium influences the conformation of the shikimate hydroxyl groups and the position of the side chains of some of the residues of the active site. Chloride seems to influence the affinity of ADP and its position in the active site and the opening length of the LID domain. Shikimate binding causes a closing of the LID domain and also seems to influence the crystallographic packing of SK. The results shown here could be useful for understanding the catalytic mechanism of SK and the role of ions in the activity of this protein.
| | The line below this paragraph, {{ABSTRACT_PUBMED_17183161}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17183161 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17183161}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Alpha/beta]] | | [[Category: Alpha/beta]] |
| [[Category: Shikimate pathway]] | | [[Category: Shikimate pathway]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 00:20:16 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 11:12:37 2008'' |
