1ok0

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{{Seed}}
 
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[[Image:1ok0.png|left|200px]]
 
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==Crystal Structure of Tendamistat==
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The line below this paragraph, containing "STRUCTURE_1ok0", creates the "Structure Box" on the page.
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<StructureSection load='1ok0' size='340' side='right'caption='[[1ok0]], [[Resolution|resolution]] 0.93&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'>[[1ok0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_tendae Streptomyces tendae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OK0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OK0 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]] 0.93&#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=GOL:GLYCEROL'>GOL</scene></td></tr>
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{{STRUCTURE_1ok0| PDB=1ok0 | 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=1ok0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ok0 OCA], [https://pdbe.org/1ok0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ok0 RCSB], [https://www.ebi.ac.uk/pdbsum/1ok0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ok0 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/IAA_STRTE IAA_STRTE] Inhibits mammalian alpha-amylases specifically but has no action on plant and microbial alpha-amylases. Forms a tight stoichiometric 1:1 complex with alpha-amylase.
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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/ok/1ok0_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1ok0 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 crystal structure of the proteinaceous alpha-amylase inhibitor tendamistat has been determined at 100 K to a resolution of 0.93 A. The final R factor for all reflections with F &gt; 4sigma(F) is 9.26%. The mean coordinate error for fully occupied protein atoms as derived from full-matrix inversion is 0.018 A. An extended network of multiple discrete conformations has been identified on the side of tendamistat that binds to the target molecule. Most notably, residue Tyr15, which interacts with the glycine-rich loop characteristic of mammalian amylases, and a cluster of amino-acid side chains surrounding it are found in two well defined conformations. The flexibility observed in this crystal structure together with information about residues fixed by lattice contacts in the crystal but found to be mobile in a previous NMR study supports a model in which most of the residues involved in binding are not fixed in the free form of the inhibitor, suggesting an induced-fit type of binding.
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===CRYSTAL STRUCTURE OF TENDAMISTAT===
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Structure of the alpha-amylase inhibitor tendamistat at 0.93 A.,Konig V, Vertesy L, Schneider TR Acta Crystallogr D Biol Crystallogr. 2003 Oct;59(Pt 10):1737-43. Epub 2003, Sep 19. PMID:14501112<ref>PMID:14501112</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_14501112}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1ok0" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 14501112 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_14501112}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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1OK0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_tendae Streptomyces tendae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OK0 OCA].
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==Reference==
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Structure of the alpha-amylase inhibitor tendamistat at 0.93 A., Konig V, Vertesy L, Schneider TR, Acta Crystallogr D Biol Crystallogr. 2003 Oct;59(Pt 10):1737-43. Epub 2003, Sep 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14501112 14501112]
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[[Category: Single protein]]
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[[Category: Streptomyces tendae]]
[[Category: Streptomyces tendae]]
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[[Category: Koenig, V.]]
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[[Category: Koenig V]]
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[[Category: Schneider, T R.]]
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[[Category: Schneider TR]]
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[[Category: Vertesy, L.]]
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[[Category: Vertesy L]]
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[[Category: Alpha amylase inhibitor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 08:49:58 2008''
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Current revision

Crystal Structure of Tendamistat

PDB ID 1ok0

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