1zui
From Proteopedia
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|PDB= 1zui |SIZE=350|CAPTION= <scene name='initialview01'>1zui</scene>, resolution 2.300Å | |PDB= 1zui |SIZE=350|CAPTION= <scene name='initialview01'>1zui</scene>, resolution 2.300Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> | + | |LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SKM:(3R,4S,5R)-3,4,5-TRIHYDROXYCYCLOHEX-1-ENE-1-CARBOXYLIC+ACID'>SKM</scene> |
| - | |ACTIVITY= [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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= AroK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=210 Helicobacter pylori]) | |GENE= AroK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=210 Helicobacter pylori]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zui FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zui OCA], [http://www.ebi.ac.uk/pdbsum/1zui PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1zui RCSB]</span> | ||
}} | }} | ||
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[[Category: Cheng, W C.]] | [[Category: Cheng, W C.]] | ||
[[Category: Wang, W C.]] | [[Category: Wang, W C.]] | ||
| - | [[Category: PO4]] | ||
| - | [[Category: SKM]] | ||
[[Category: alpha-beta protein]] | [[Category: alpha-beta protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:41:47 2008'' |
Revision as of 22:41, 30 March 2008
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| , resolution 2.300Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | AroK (Helicobacter pylori) | ||||||
| Activity: | Shikimate kinase, with EC number 2.7.1.71 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structural Basis for Shikimate-binding Specificity of Helicobacter pylori Shikimate Kinase
Overview
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
1ZUI is a Single protein structure of sequence from Helicobacter pylori. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Mon Mar 31 01:41:47 2008
