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2iyy

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[[Image:2iyy.gif|left|200px]]
 
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==Shikimate kinase from Mycobacterium tuberculosis in complex with shikimate-3-phosphate and SO4==
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The line below this paragraph, containing "STRUCTURE_2iyy", creates the "Structure Box" on the page.
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<StructureSection load='2iyy' size='340' side='right'caption='[[2iyy]], [[Resolution|resolution]] 1.62&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2iyy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IYY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IYY FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.62&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=S3P:SHIKIMATE-3-PHOSPHATE'>S3P</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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{{STRUCTURE_2iyy| PDB=2iyy | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2iyy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iyy OCA], [https://pdbe.org/2iyy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2iyy RCSB], [https://www.ebi.ac.uk/pdbsum/2iyy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2iyy ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/AROK_MYCTU AROK_MYCTU] Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.<ref>PMID:11483005</ref> <ref>PMID:17020768</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/iy/2iyy_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2iyy ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The structural mechanism of the catalytic functioning of shikimate kinase from Mycobacterium tuberculosis was investigated on the basis of a series of high-resolution crystal structures corresponding to individual steps in the enzymatic reaction. The catalytic turnover of shikimate and ATP into the products shikimate-3-phosphate and ADP, followed by release of ADP, was studied in the crystalline environment. Based on a comparison of the structural states before initiation of the reaction and immediately after the catalytic step, we derived a structural model of the transition state that suggests that phosphoryl transfer proceeds with inversion by an in-line associative mechanism. The random sequential binding of shikimate and nucleotides is associated with domain movements. We identified a synergic mechanism by which binding of the first substrate may enhance the affinity for the second substrate.
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'''SHIKIMATE KINASE FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX WITH SHIKIMATE-3-PHOSPHATE AND SO4'''
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Mechanism of phosphoryl transfer catalyzed by shikimate kinase from Mycobacterium tuberculosis.,Hartmann MD, Bourenkov GP, Oberschall A, Strizhov N, Bartunik HD J Mol Biol. 2006 Dec 1;364(3):411-23. Epub 2006 Sep 5. PMID:17020768<ref>PMID:17020768</ref>
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==Overview==
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The structural mechanism of the catalytic functioning of shikimate kinase from Mycobacterium tuberculosis was investigated on the basis of a series of high-resolution crystal structures corresponding to individual steps in the enzymatic reaction. The catalytic turnover of shikimate and ATP into the products shikimate-3-phosphate and ADP, followed by release of ADP, was studied in the crystalline environment. Based on a comparison of the structural states before initiation of the reaction and immediately after the catalytic step, we derived a structural model of the transition state that suggests that phosphoryl transfer proceeds with inversion by an in-line associative mechanism. The random sequential binding of shikimate and nucleotides is associated with domain movements. We identified a synergic mechanism by which binding of the first substrate may enhance the affinity for the second substrate.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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2IYY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IYY OCA].
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</div>
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<div class="pdbe-citations 2iyy" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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Mechanism of phosphoryl transfer catalyzed by shikimate kinase from Mycobacterium tuberculosis., Hartmann MD, Bourenkov GP, Oberschall A, Strizhov N, Bartunik HD, J Mol Biol. 2006 Dec 1;364(3):411-23. Epub 2006 Sep 5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17020768 17020768]
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*[[Shikimate kinase 3D structures|Shikimate kinase 3D structures]]
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[[Category: Mycobacterium tuberculosis]]
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== References ==
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[[Category: Shikimate kinase]]
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<references/>
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[[Category: Single protein]]
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__TOC__
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[[Category: Bartunik, H D.]]
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</StructureSection>
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[[Category: Bourenkov, G P.]]
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[[Category: Large Structures]]
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[[Category: Hartmann, M D.]]
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[[Category: Mycobacterium tuberculosis H37Rv]]
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[[Category: Oberschall, A.]]
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[[Category: Bartunik HD]]
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[[Category: Strizhov, N.]]
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[[Category: Bourenkov GP]]
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[[Category: Amino-acid biosynthesis]]
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[[Category: Hartmann MD]]
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[[Category: Aromatic amino acid biosynthesis]]
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[[Category: Oberschall A]]
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[[Category: Atp-binding]]
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[[Category: Strizhov N]]
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[[Category: Kinase]]
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[[Category: Magnesium]]
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[[Category: Metal-binding]]
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[[Category: Nucleotide-binding]]
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[[Category: P-loop kinase]]
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[[Category: Shikimate kinase]]
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[[Category: Shikimate pathway]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 08:05:54 2008''
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Current revision

Shikimate kinase from Mycobacterium tuberculosis in complex with shikimate-3-phosphate and SO4

PDB ID 2iyy

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