1m44

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(New page: 200px<br /><applet load="1m44" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m44, resolution 1.6&Aring;" /> '''Aminoglycoside 2'-N-a...)
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[[Image:1m44.gif|left|200px]]<br /><applet load="1m44" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1m44.gif|left|200px]]<br /><applet load="1m44" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1m44, resolution 1.6&Aring;" />
caption="1m44, resolution 1.6&Aring;" />
'''Aminoglycoside 2'-N-acetyltransferase from Mycobacterium tuberculosis-APO Structure'''<br />
'''Aminoglycoside 2'-N-acetyltransferase from Mycobacterium tuberculosis-APO Structure'''<br />
==Overview==
==Overview==
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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.
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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==
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1M44 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 SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1M44 OCA].
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1M44 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=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M44 OCA].
==Reference==
==Reference==
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[[Category: Mycobacterium tuberculosis]]
[[Category: Mycobacterium tuberculosis]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Blanchard, J.S.]]
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[[Category: Blanchard, J S.]]
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[[Category: Hegde, S.S.]]
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[[Category: Hegde, S S.]]
[[Category: Javid-Majd, F.]]
[[Category: Javid-Majd, F.]]
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[[Category: Roderick, S.L.]]
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[[Category: Roderick, S L.]]
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[[Category: Vetting, M.W.]]
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[[Category: Vetting, M W.]]
[[Category: SO4]]
[[Category: SO4]]
[[Category: coa binding motif]]
[[Category: coa binding motif]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:07:57 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:51:13 2008''

Revision as of 11:51, 21 February 2008


1m44, resolution 1.6Å

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Aminoglycoside 2'-N-acetyltransferase from Mycobacterium tuberculosis-APO Structure

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

1M44 is a Single protein structure of sequence from Mycobacterium tuberculosis with as ligand. 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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