1i1d: Difference between revisions

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[[Image:1i1d.gif|left|200px]]<br /><applet load="1i1d" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1i1d.gif|left|200px]]<br /><applet load="1i1d" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1i1d, resolution 1.80Å" />

'''CRYSTAL STRUCTURE OF YEAST GNA1 BOUND TO COA AND GLNAC-6P'''<br />

==Overview==

The yeast enzymes involved in UDP-GlcNAc biosynthesis are potential, targets for antifungal agents. GNA1, a novel member of the Gcn5-related, N-acetyltransferase (GNAT) superfamily, participates in UDP-GlcNAc, biosynthesis by catalyzing the formation of GlcNAc6P from AcCoA and, GlcN6P. We have solved three crystal structures corresponding to the apo, Saccharomyces cerevisiae GNA1, the GNA1-AcCoA, and the GNA1-CoA-GlcNAc6P, complexes and have refined them to 2.4, 1.3, and 1.8 A resolution, respectively. These structures not only reveal a stable, beta-intertwined, dimeric assembly with the GlcNAc6P binding site located at the dimer, interface but also shed light on the catalytic machinery of GNA1 at an, atomic level. Hence, they broaden our understanding of structural features, required for GNAT activity, provide structural details for related, aminoglycoside N-acetyltransferases, and highlight the adaptability of the, GNAT superfamily members to acquire various specificities.

The yeast enzymes involved in UDP-GlcNAc biosynthesis are potential targets for antifungal agents. GNA1, a novel member of the Gcn5-related N-acetyltransferase (GNAT) superfamily, participates in UDP-GlcNAc biosynthesis by catalyzing the formation of GlcNAc6P from AcCoA and GlcN6P. We have solved three crystal structures corresponding to the apo Saccharomyces cerevisiae GNA1, the GNA1-AcCoA, and the GNA1-CoA-GlcNAc6P complexes and have refined them to 2.4, 1.3, and 1.8 A resolution, respectively. These structures not only reveal a stable, beta-intertwined, dimeric assembly with the GlcNAc6P binding site located at the dimer interface but also shed light on the catalytic machinery of GNA1 at an atomic level. Hence, they broaden our understanding of structural features required for GNAT activity, provide structural details for related aminoglycoside N-acetyltransferases, and highlight the adaptability of the GNAT superfamily members to acquire various specificities.

==About this Structure==

1I1D is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with 16G, COA and IMD as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Glucosamine_6-phosphate_N-acetyltransferase Glucosamine 6-phosphate N-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.4 2.3.1.4] Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1I1D OCA].

1I1D is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=16G:'>16G</scene>, <scene name='pdbligand=COA:'>COA</scene> and <scene name='pdbligand=IMD:'>IMD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Glucosamine_6-phosphate_N-acetyltransferase Glucosamine 6-phosphate N-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.4 2.3.1.4] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I1D OCA].

==Reference==

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[[Category: gnat conserved core]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:06:57 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1i1d.gif|left|200px]]<br /><applet load="1i1d" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1i1d.gif|left|200px]]<br /><applet load="1i1d" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1i1d, resolution 1.80&Aring;" />
 '''CRYSTAL STRUCTURE OF YEAST GNA1 BOUND TO COA AND GLNAC-6P'''<br />
 ==Overview==
-The yeast enzymes involved in UDP-GlcNAc biosynthesis are potential, targets for antifungal agents. GNA1, a novel member of the Gcn5-related, N-acetyltransferase (GNAT) superfamily, participates in UDP-GlcNAc, biosynthesis by catalyzing the formation of GlcNAc6P from AcCoA and, GlcN6P. We have solved three crystal structures corresponding to the apo, Saccharomyces cerevisiae GNA1, the GNA1-AcCoA, and the GNA1-CoA-GlcNAc6P, complexes and have refined them to 2.4, 1.3, and 1.8 A resolution, respectively. These structures not only reveal a stable, beta-intertwined, dimeric assembly with the GlcNAc6P binding site located at the dimer, interface but also shed light on the catalytic machinery of GNA1 at an, atomic level. Hence, they broaden our understanding of structural features, required for GNAT activity, provide structural details for related, aminoglycoside N-acetyltransferases, and highlight the adaptability of the, GNAT superfamily members to acquire various specificities.
+The yeast enzymes involved in UDP-GlcNAc biosynthesis are potential targets for antifungal agents. GNA1, a novel member of the Gcn5-related N-acetyltransferase (GNAT) superfamily, participates in UDP-GlcNAc biosynthesis by catalyzing the formation of GlcNAc6P from AcCoA and GlcN6P. We have solved three crystal structures corresponding to the apo Saccharomyces cerevisiae GNA1, the GNA1-AcCoA, and the GNA1-CoA-GlcNAc6P complexes and have refined them to 2.4, 1.3, and 1.8 A resolution, respectively. These structures not only reveal a stable, beta-intertwined, dimeric assembly with the GlcNAc6P binding site located at the dimer interface but also shed light on the catalytic machinery of GNA1 at an atomic level. Hence, they broaden our understanding of structural features required for GNAT activity, provide structural details for related aminoglycoside N-acetyltransferases, and highlight the adaptability of the GNAT superfamily members to acquire various specificities.
 ==About this Structure==
-I1D is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with 16G, COA and IMD as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Glucosamine_6-phosphate_N-acetyltransferase Glucosamine 6-phosphate N-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.4 2.3.1.4] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1I1D OCA].
+I1D is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=16G:'>16G</scene>, <scene name='pdbligand=COA:'>COA</scene> and <scene name='pdbligand=IMD:'>IMD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Glucosamine_6-phosphate_N-acetyltransferase Glucosamine 6-phosphate N-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.4 2.3.1.4] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I1D OCA].
 ==Reference==
@@ Line 24: / Line 24: @@
 [[Category: gnat conserved core]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:58:16 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:06:57 2008''