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1zui

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Revision as of 10:24, 12 October 2017

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

Structural highlights

1zui is a 1 chain structure with sequence from Campylobacter pylori. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Gene:	AroK (Campylobacter pylori)
Activity:	Shikimate kinase, with EC number 2.7.1.71
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.

Publication Abstract from PubMed

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.

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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ 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
↑ 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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1zui"

@@ Line 1: / Line 1: @@
 ==Structural Basis for Shikimate-binding Specificity of Helicobacter pylori Shikimate Kinase==
 <StructureSection load='1zui' size='340' side='right' caption='[[1zui]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AroK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=85962 Campylobacter pylori])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1zui PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1zui RCSB], [http://www.ebi.ac.uk/pdbsum/1zui PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1zui PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1zui RCSB], [http://www.ebi.ac.uk/pdbsum/1zui PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1zui ProSAT]</span></td></tr>
 </table>
 == Function ==

1zui

From Proteopedia

Revision as of 10:24, 12 October 2017

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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