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1m4g
From Proteopedia
(New page: 200px<br /><applet load="1m4g" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m4g, resolution 1.8Å" /> '''Aminoglycoside 2'-N-a...) |
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| - | [[Image:1m4g.jpg|left|200px]]<br /><applet load="1m4g" size=" | + | [[Image:1m4g.jpg|left|200px]]<br /><applet load="1m4g" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1m4g, resolution 1.8Å" /> | caption="1m4g, resolution 1.8Å" /> | ||
'''Aminoglycoside 2'-N-acetyltransferase from Mycobacterium tuberculosis-Complex with Coenzyme A and Ribostamycin'''<br /> | '''Aminoglycoside 2'-N-acetyltransferase from Mycobacterium tuberculosis-Complex with Coenzyme A and Ribostamycin'''<br /> | ||
==Overview== | ==Overview== | ||
| - | AAC(2')-Ic catalyzes the coenzyme A (CoA)-dependent acetylation of the 2' | + | AAC(2')-Ic catalyzes the coenzyme A (CoA)-dependent acetylation of the 2' hydroxyl or amino group of a broad spectrum of aminoglycosides. The crystal structure of the AAC(2')-Ic from Mycobacterium tuberculosis has been determined in the apo enzyme form and in ternary complexes with CoA and either tobramycin, kanamycin A or ribostamycin, representing the first structures of an aminoglycoside acetyltransferase bound to a drug. The overall fold of AAC(2')-Ic places it in the GCN5-related N-acetyltransferase (GNAT) superfamily. Although the physiological function of AAC(2')-Ic is uncertain, a structural analysis of these high-affinity aminoglycoside complexes suggests that the enzyme may acetylate a key biosynthetic intermediate of mycothiol, the major reducing agent in mycobacteria, and participate in the regulation of cellular redox potential. |
==About this Structure== | ==About this Structure== | ||
| - | 1M4G is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis] with COA, RIO and PAP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1M4G is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis] with <scene name='pdbligand=COA:'>COA</scene>, <scene name='pdbligand=RIO:'>RIO</scene> and <scene name='pdbligand=PAP:'>PAP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M4G OCA]. |
==Reference== | ==Reference== | ||
| Line 13: | Line 13: | ||
[[Category: Mycobacterium tuberculosis]] | [[Category: Mycobacterium tuberculosis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Blanchard, J | + | [[Category: Blanchard, J S.]] |
| - | [[Category: Hegde, S | + | [[Category: Hegde, S S.]] |
[[Category: Javid-Majd, F.]] | [[Category: Javid-Majd, F.]] | ||
| - | [[Category: Roderick, S | + | [[Category: Roderick, S L.]] |
| - | [[Category: Vetting, M | + | [[Category: Vetting, M W.]] |
[[Category: COA]] | [[Category: COA]] | ||
[[Category: PAP]] | [[Category: PAP]] | ||
| Line 23: | Line 23: | ||
[[Category: coa binding motif]] | [[Category: coa binding motif]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:51:18 2008'' |
Revision as of 11:51, 21 February 2008
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Aminoglycoside 2'-N-acetyltransferase from Mycobacterium tuberculosis-Complex with Coenzyme A and Ribostamycin
Overview
AAC(2')-Ic catalyzes the coenzyme A (CoA)-dependent acetylation of the 2' hydroxyl or amino group of a broad spectrum of aminoglycosides. The crystal structure of the AAC(2')-Ic from Mycobacterium tuberculosis has been determined in the apo enzyme form and in ternary complexes with CoA and either tobramycin, kanamycin A or ribostamycin, representing the first structures of an aminoglycoside acetyltransferase bound to a drug. The overall fold of AAC(2')-Ic places it in the GCN5-related N-acetyltransferase (GNAT) superfamily. Although the physiological function of AAC(2')-Ic is uncertain, a structural analysis of these high-affinity aminoglycoside complexes suggests that the enzyme may acetylate a key biosynthetic intermediate of mycothiol, the major reducing agent in mycobacteria, and participate in the regulation of cellular redox potential.
About this Structure
1M4G is a Single protein structure of sequence from Mycobacterium tuberculosis with , and as ligands. Full crystallographic information is available from OCA.
Reference
Aminoglycoside 2'-N-acetyltransferase from Mycobacterium tuberculosis in complex with coenzyme A and aminoglycoside substrates., Vetting MW, Hegde SS, Javid-Majd F, Blanchard JS, Roderick SL, Nat Struct Biol. 2002 Sep;9(9):653-8. PMID:12161746
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