1yk3
From Proteopedia
(New page: 200px<br /><applet load="1yk3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yk3, resolution 2.20Å" /> '''Crystal structure of...) |
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| - | [[Image:1yk3.gif|left|200px]]<br /><applet load="1yk3" size=" | + | [[Image:1yk3.gif|left|200px]]<br /><applet load="1yk3" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1yk3, resolution 2.20Å" /> | caption="1yk3, resolution 2.20Å" /> | ||
'''Crystal structure of Rv1347c from Mycobacterium tuberculosis'''<br /> | '''Crystal structure of Rv1347c from Mycobacterium tuberculosis'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Mycobacterium tuberculosis, the cause of tuberculosis, is a devastating | + | Mycobacterium tuberculosis, the cause of tuberculosis, is a devastating human pathogen. The emergence of multidrug resistance in recent years has prompted a search for new drug targets and for a better understanding of mechanisms of resistance. Here we focus on the gene product of an open reading frame from M. tuberculosis, Rv1347c, which is annotated as a putative aminoglycoside N-acetyltransferase. The Rv1347c protein does not show this activity, however, and we show from its crystal structure, coupled with functional and bioinformatic data, that its most likely role is in the biosynthesis of mycobactin, the M. tuberculosis siderophore. The crystal structure of Rv1347c was determined by multiwavelength anomalous diffraction phasing from selenomethionine-substituted protein and refined at 2.2 angstrom resolution (r = 0.227, R(free) = 0.257). The protein is monomeric, with a fold that places it in the GCN5-related N-acetyltransferase (GNAT) family of acyltransferases. Features of the structure are an acyl-CoA binding site that is shared with other GNAT family members and an adjacent hydrophobic channel leading to the surface that could accommodate long-chain acyl groups. Modeling the postulated substrate, the N(epsilon)-hydroxylysine side chain of mycobactin, into the acceptor substrate binding groove identifies two residues at the active site, His130 and Asp168, that have putative roles in substrate binding and catalysis. |
==About this Structure== | ==About this Structure== | ||
| - | 1YK3 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 BOG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1YK3 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=BOG:'>BOG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YK3 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Mycobacterium tuberculosis]] | [[Category: Mycobacterium tuberculosis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Baker, E | + | [[Category: Baker, E N.]] |
| - | [[Category: Card, G | + | [[Category: Card, G L.]] |
| - | [[Category: Peterson, N | + | [[Category: Peterson, N A.]] |
[[Category: Rupp, B.]] | [[Category: Rupp, B.]] | ||
| - | [[Category: Schick, B | + | [[Category: Schick, B M.]] |
| - | [[Category: Smith, C | + | [[Category: Smith, C A.]] |
| - | [[Category: TBSGC, TB | + | [[Category: TBSGC, TB Structural Genomics Consortium.]] |
[[Category: BOG]] | [[Category: BOG]] | ||
[[Category: acyltransferase]] | [[Category: acyltransferase]] | ||
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[[Category: tbsgc]] | [[Category: tbsgc]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:06:08 2008'' |
Revision as of 14:06, 21 February 2008
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Crystal structure of Rv1347c from Mycobacterium tuberculosis
Overview
Mycobacterium tuberculosis, the cause of tuberculosis, is a devastating human pathogen. The emergence of multidrug resistance in recent years has prompted a search for new drug targets and for a better understanding of mechanisms of resistance. Here we focus on the gene product of an open reading frame from M. tuberculosis, Rv1347c, which is annotated as a putative aminoglycoside N-acetyltransferase. The Rv1347c protein does not show this activity, however, and we show from its crystal structure, coupled with functional and bioinformatic data, that its most likely role is in the biosynthesis of mycobactin, the M. tuberculosis siderophore. The crystal structure of Rv1347c was determined by multiwavelength anomalous diffraction phasing from selenomethionine-substituted protein and refined at 2.2 angstrom resolution (r = 0.227, R(free) = 0.257). The protein is monomeric, with a fold that places it in the GCN5-related N-acetyltransferase (GNAT) family of acyltransferases. Features of the structure are an acyl-CoA binding site that is shared with other GNAT family members and an adjacent hydrophobic channel leading to the surface that could accommodate long-chain acyl groups. Modeling the postulated substrate, the N(epsilon)-hydroxylysine side chain of mycobactin, into the acceptor substrate binding groove identifies two residues at the active site, His130 and Asp168, that have putative roles in substrate binding and catalysis.
About this Structure
1YK3 is a Single protein structure of sequence from Mycobacterium tuberculosis with as ligand. Full crystallographic information is available from OCA.
Reference
The crystal structure of Rv1347c, a putative antibiotic resistance protein from Mycobacterium tuberculosis, reveals a GCN5-related fold and suggests an alternative function in siderophore biosynthesis., Card GL, Peterson NA, Smith CA, Rupp B, Schick BM, Baker EN, J Biol Chem. 2005 Apr 8;280(14):13978-86. Epub 2005 Jan 28. PMID:15695811
Page seeded by OCA on Thu Feb 21 16:06:08 2008
Categories: Mycobacterium tuberculosis | Single protein | Baker, E N. | Card, G L. | Peterson, N A. | Rupp, B. | Schick, B M. | Smith, C A. | TBSGC, TB Structural Genomics Consortium. | BOG | Acyltransferase | Gcn5-related fold | Protein structure initiative | Psi | Structural genomics | Tb structural genomics consortium | Tbsgc
