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1l2l

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(New page: 200px<br /><applet load="1l2l" size="450" color="white" frame="true" align="right" spinBox="true" caption="1l2l, resolution 2.00&Aring;" /> '''Crystal structure of...)
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[[Image:1l2l.gif|left|200px]]<br /><applet load="1l2l" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1l2l, resolution 2.00&Aring;" />
 
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'''Crystal structure of ADP-dependent glucokinase from a Pyrococcus Horikoshii'''<br />
 
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==Overview==
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==Crystal structure of ADP-dependent glucokinase from a Pyrococcus Horikoshii==
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Although ATP is the most common phosphoryl group donor for kinases, some, kinases from certain hyperthermophilic archaea such as Pyrococcus, horikoshii and Thermococcus litoralis use ADP as the phosphoryl donor., Those are ADP-dependent glucokinases (ADPGK) and phosphofructokinases in, their glycolytic pathway. Here, we succeeded in gene cloning the ADPGK, from P. horikoshii OT3 (phGK) in Escherichia coli,and in easy preparation, of the enzyme, crystallization, and the structure determination of the apo, enzyme. Recently, the three-dimensional structure of the ADPGK from T., litoralis (tlGK) in a complex with ADP was reported. The overall structure, of two homologous enzymes (56.7%) was basically similar: This means that, they consisted of large alpha/beta-domains and small domains. However, a, marked adjustment of the two domains, which is a 10-A translation and a 20, degrees rotation from the conserved GG sequence located at the center of, the hinge, was observed between the apo-phGK and ADP-tlGK structures. The, ADP-binding loop (430-439) was disordered in the apo form. It is suggested, that a large conformational change takes place during the enzymatic, reaction.
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<StructureSection load='1l2l' size='340' side='right'caption='[[1l2l]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1l2l]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L2L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L2L FirstGlance]. <br>
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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]] 2&#8491;</td></tr>
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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=1l2l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l2l OCA], [https://pdbe.org/1l2l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l2l RCSB], [https://www.ebi.ac.uk/pdbsum/1l2l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l2l ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GLKA_PYRHO GLKA_PYRHO] Catalyzes the phosphorylation of D-glucose to D-glucose 6-phosphate using ADP as the phosphate donor.
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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/l2/1l2l_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=1l2l ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1L2L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii]. Active as [http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1L2L OCA].
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*[[Hexokinase 3D structures|Hexokinase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Crystal structure of the ADP-dependent glucokinase from Pyrococcus horikoshii at 2.0-A resolution: a large conformational change in ADP-dependent glucokinase., Tsuge H, Sakuraba H, Kobe T, Kujime A, Katunuma N, Ohshima T, Protein Sci. 2002 Oct;11(10):2456-63. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12237466 12237466]
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[[Category: Large Structures]]
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[[Category: Glucokinase]]
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[[Category: Pyrococcus horikoshii]]
[[Category: Pyrococcus horikoshii]]
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[[Category: Single protein]]
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[[Category: Katunuma N]]
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[[Category: Katunuma, N.]]
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[[Category: Ohshima T]]
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[[Category: Ohshima, T.]]
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[[Category: Sakuraba H]]
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[[Category: Sakuraba, H.]]
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[[Category: Tsuge H]]
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[[Category: Tsuge, H.]]
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[[Category: adp glucokinase apo]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:11:31 2007''
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Current revision

Crystal structure of ADP-dependent glucokinase from a Pyrococcus Horikoshii

PDB ID 1l2l

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