1zui: Difference between revisions
New page: left|200px<br /><applet load="1zui" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zui, resolution 2.300Å" /> '''Structural Basis fo... |
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[[Image:1zui.gif|left|200px]]<br /><applet load="1zui" size=" | [[Image:1zui.gif|left|200px]]<br /><applet load="1zui" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1zui, resolution 2.300Å" /> | caption="1zui, resolution 2.300Å" /> | ||
'''Structural Basis for Shikimate-binding Specificity of Helicobacter pylori Shikimate Kinase'''<br /> | '''Structural Basis for Shikimate-binding Specificity of Helicobacter pylori Shikimate Kinase'''<br /> | ||
==Overview== | ==Overview== | ||
Shikimate kinase (EC 2.7.1.71) catalyzes the specific phosphorylation of | Shikimate kinase (EC 2.7.1.71) catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid in the presence of ATP. As the fifth key step in the shikimate pathway for aromatic amino acid biosynthesis in bacteria, fungi, and plants, but not mammals, shikimate kinase represents an attractive target for the development of new antimicrobial agents, herbicides, and antiparasitic agents. Here, we report the 1.8-Angstroms crystal structure of Helicobacter pylori shikimate kinase (HpSK). The crystal structure shows a three-layer alpha/beta fold consisting of a central sheet of five parallel beta-strands flanked by seven alpha-helices. An HpSK-shikimate-PO(4) complex was also determined and refined to 2.3 Angstroms, revealing induced-fit movement from an open to a closed form on substrate binding. Shikimate is located above a short 3(10) helix formed by a strictly conserved motif (GGGXV) after beta(3). Moreover, several highly conserved charged residues including Asp33 (in a conserved DT/SD motif), Arg57, and Arg132 (interacting with shikimate) are identified, guiding the development of novel inhibitors of shikimate kinase. | ||
==About this Structure== | ==About this Structure== | ||
1ZUI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori] with PO4 and SKM as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Shikimate_kinase Shikimate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.71 2.7.1.71] Full crystallographic information is available from [http:// | 1ZUI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori] with <scene name='pdbligand=PO4:'>PO4</scene> and <scene name='pdbligand=SKM:'>SKM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Shikimate_kinase Shikimate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.71 2.7.1.71] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZUI OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Shikimate kinase]] | [[Category: Shikimate kinase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Chang, Y | [[Category: Chang, Y N.]] | ||
[[Category: Cheng, W | [[Category: Cheng, W C.]] | ||
[[Category: Wang, W | [[Category: Wang, W C.]] | ||
[[Category: PO4]] | [[Category: PO4]] | ||
[[Category: SKM]] | [[Category: SKM]] | ||
[[Category: alpha-beta protein]] | [[Category: alpha-beta protein]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:19:10 2008'' | ||
Revision as of 17:19, 21 February 2008
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Structural Basis for Shikimate-binding Specificity of Helicobacter pylori Shikimate Kinase
OverviewOverview
Shikimate kinase (EC 2.7.1.71) catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid in the presence of ATP. As the fifth key step in the shikimate pathway for aromatic amino acid biosynthesis in bacteria, fungi, and plants, but not mammals, shikimate kinase represents an attractive target for the development of new antimicrobial agents, herbicides, and antiparasitic agents. Here, we report the 1.8-Angstroms crystal structure of Helicobacter pylori shikimate kinase (HpSK). The crystal structure shows a three-layer alpha/beta fold consisting of a central sheet of five parallel beta-strands flanked by seven alpha-helices. An HpSK-shikimate-PO(4) complex was also determined and refined to 2.3 Angstroms, revealing induced-fit movement from an open to a closed form on substrate binding. Shikimate is located above a short 3(10) helix formed by a strictly conserved motif (GGGXV) after beta(3). Moreover, several highly conserved charged residues including Asp33 (in a conserved DT/SD motif), Arg57, and Arg132 (interacting with shikimate) are identified, guiding the development of novel inhibitors of shikimate kinase.
About this StructureAbout this Structure
1ZUI is a Single protein structure of sequence from Helicobacter pylori with and as ligands. Active as Shikimate kinase, with EC number 2.7.1.71 Full crystallographic information is available from OCA.
ReferenceReference
Structural basis for shikimate-binding specificity of Helicobacter pylori shikimate kinase., Cheng WC, Chang YN, Wang WC, J Bacteriol. 2005 Dec;187(23):8156-63. PMID:16291688
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