2fk8
From Proteopedia
| Line 7: | Line 7: | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= mmaA4 (Rv0642c) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 Mycobacterium tuberculosis]) | |GENE= mmaA4 (Rv0642c) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 Mycobacterium tuberculosis]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2fk7|2FK7]], [[1kp9|1KP9]], [[1kpg|1KPG]], [[1kph|1KPH]], [[1kpi|1KPI]], [[1l1e|1L1E]], [[1tpy|1TPY]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fk8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fk8 OCA], [http://www.ebi.ac.uk/pdbsum/2fk8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2fk8 RCSB]</span> | ||
}} | }} | ||
| Line 25: | Line 28: | ||
[[Category: Guillet, V.]] | [[Category: Guillet, V.]] | ||
[[Category: Mourey, L.]] | [[Category: Mourey, L.]] | ||
| - | [[Category: SAM]] | ||
[[Category: s-adenosylmethionine-dependent methyltransferase fold]] | [[Category: s-adenosylmethionine-dependent methyltransferase fold]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:03:57 2008'' |
Revision as of 00:03, 31 March 2008
| |||||||
| , resolution 2.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | mmaA4 (Rv0642c) (Mycobacterium tuberculosis) | ||||||
| Related: | 2FK7, 1KP9, 1KPG, 1KPH, 1KPI, 1L1E, 1TPY
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of Hma (MmaA4) from Mycobacterium tuberculosis complexed with S-adenosylmethionine
Overview
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.
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
Page seeded by OCA on Mon Mar 31 03:03:57 2008
