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[[Image:1zui.gif|left|200px]]


{{Structure
==Structural Basis for Shikimate-binding Specificity of Helicobacter pylori Shikimate Kinase==
|PDB= 1zui |SIZE=350|CAPTION= <scene name='initialview01'>1zui</scene>, resolution 2.300&Aring;
<StructureSection load='1zui' size='340' side='right'caption='[[1zui]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> and <scene name='pdbligand=SKM:(3R,4S,5R)-3,4,5-TRIHYDROXYCYCLOHEX-1-ENE-1-CARBOXYLIC ACID'>SKM</scene>
<table><tr><td colspan='2'>[[1zui]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori_26695 Helicobacter pylori 26695]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZUI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZUI FirstGlance]. <br>
|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]  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
|GENE= AroK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=210 Helicobacter pylori])
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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></td></tr>
}}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1zui FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zui OCA], [https://pdbe.org/1zui PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zui RCSB], [https://www.ebi.ac.uk/pdbsum/1zui PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zui ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/AROK_HELPY AROK_HELPY] Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.<ref>PMID:16291688</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zu/1zui_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1zui ConSurf].
<div style="clear:both"></div>


'''Structural Basis for Shikimate-binding Specificity of Helicobacter pylori Shikimate Kinase'''
==See Also==
 
*[[Shikimate kinase 3D structures|Shikimate kinase 3D structures]]
 
== References ==
==Overview==
<references/>
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.
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Helicobacter pylori 26695]]
1ZUI is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZUI OCA].
[[Category: Large Structures]]
 
[[Category: Chang YN]]
==Reference==
[[Category: Cheng WC]]
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:[http://www.ncbi.nlm.nih.gov/pubmed/16291688 16291688]
[[Category: Wang WC]]
[[Category: Helicobacter pylori]]
[[Category: Shikimate kinase]]
[[Category: Single protein]]
[[Category: Chang, Y N.]]
[[Category: Cheng, W C.]]
[[Category: Wang, W C.]]
[[Category: PO4]]
[[Category: SKM]]
[[Category: alpha-beta protein]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:39:58 2008''

Latest revision as of 16:39, 13 March 2024

Structural Basis for Shikimate-binding Specificity of Helicobacter pylori Shikimate KinaseStructural Basis for Shikimate-binding Specificity of Helicobacter pylori Shikimate Kinase

Structural highlights

1zui is a 1 chain structure with sequence from Helicobacter pylori 26695. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.3Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

AROK_HELPY Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Cheng WC, Chang YN, Wang WC. Structural basis for shikimate-binding specificity of Helicobacter pylori shikimate kinase. J Bacteriol. 2005 Dec;187(23):8156-63. PMID:16291688 doi:187/23/8156

1zui, resolution 2.30Å

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