1i12: Difference between revisions

Line 1:

[[Image:1i12.~~jpg~~|left|200px]]

[[Image:1i12.png|left|200px]]

<!--

Line 9:

Line 10:

~~'''~~CRYSTAL STRUCTURE OF SACCHAROMYCES CEREVISIAE GNA1 COMPLEXED WITH ACCOA~~'''~~

===CRYSTAL STRUCTURE OF SACCHAROMYCES CEREVISIAE GNA1 COMPLEXED WITH ACCOA===

~~==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 line below this paragraph, {{ABSTRACT_PUBMED_11278591}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 11278591 is the PubMed ID number.

-->

==About this Structure==

Line 28:

Line 32:

[[Category: Alpha/beta]]

[[Category: Gnat]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ ~~2 19~~:26:56 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 10:15:14 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-[[Image:1i12.jpg|left|200px]]
+{{Seed}}
+[[Image:1i12.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1i12|  PDB=1i12  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF SACCHAROMYCES CEREVISIAE GNA1 COMPLEXED WITH ACCOA'''
+===CRYSTAL STRUCTURE OF SACCHAROMYCES CEREVISIAE GNA1 COMPLEXED WITH ACCOA===
-==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 line below this paragraph, {{ABSTRACT_PUBMED_11278591}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11278591 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11278591}}
 ==About this Structure==
@@ Line 28: / Line 32: @@
 [[Category: Alpha/beta]]
 [[Category: Gnat]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 19:26:56 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 10:15:14 2008''