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| - | [[Image:2fk8.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2fk8| PDB=2fk8 | SCENE= }} | | {{STRUCTURE_2fk8| PDB=2fk8 | SCENE= }} |
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| - | '''Crystal structure of Hma (MmaA4) from Mycobacterium tuberculosis complexed with S-adenosylmethionine'''
| + | ===Crystal structure of Hma (MmaA4) from Mycobacterium tuberculosis complexed with S-adenosylmethionine=== |
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| - | ==Overview==
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| - | Mycolic acids are major and specific components of the cell envelope of Mycobacteria that include Mycobacterium tuberculosis, the causative agent of tuberculosis. Their metabolism is the target of the most efficient antitubercular drug currently used in therapy, and the enzymes that are involved in the production of mycolic acids represent important targets for the development of new drugs effective against multidrug-resistant strains. Among these are the S-adenosylmethionine-dependent methyltransferases (SAM-MTs) that catalyze the introduction of key chemical modifications in defined positions of mycolic acids. Some of these subtle structural variations are known to be crucial for both the virulence of the tubercle bacillus and the permeability of the mycobacterial cell envelope. We report here the structural characterization of the enzyme Hma (MmaA4), a SAM-MT that is unique in catalyzing the introduction of a methyl branch together with an adjacent hydroxyl group essential for the formation of both keto- and methoxymycolates in M. tuberculosis. Despite the high propensity of Hma to proteolytic degradation, the enzyme was produced and crystallized, and its three-dimensional structure in the apoform and in complex with S-adenosylmethionine was solved to about 2 A. Thestructuresshowtheimportantroleplayedbythemodificationsfound within mycolic acid SAM-MTs, especially thealpha2-alpha3 motif and the chemical environment of the active site. Essential information with respect to cofactor and substrate binding, selectivity and specificity, and about the mechanism of catalytic reaction were derived.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_16356931}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16356931 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_16356931}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Mourey, L.]] | | [[Category: Mourey, L.]] |
| | [[Category: S-adenosylmethionine-dependent methyltransferase fold]] | | [[Category: S-adenosylmethionine-dependent methyltransferase fold]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:59:38 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 20:37:48 2008'' |
Revision as of 17:37, 28 July 2008
Template:STRUCTURE 2fk8
Crystal structure of Hma (MmaA4) from Mycobacterium tuberculosis complexed with S-adenosylmethionine
Template:ABSTRACT PUBMED 16356931
About this Structure
2FK8 is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.
Reference
Further insight into S-adenosylmethionine-dependent methyltransferases: structural characterization of Hma, an enzyme essential for the biosynthesis of oxygenated mycolic acids in Mycobacterium tuberculosis., Boissier F, Bardou F, Guillet V, Uttenweiler-Joseph S, Daffe M, Quemard A, Mourey L, J Biol Chem. 2006 Feb 17;281(7):4434-45. Epub 2005 Dec 15. PMID:16356931
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