1hkb

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(New page: 200px<br /> <applet load="1hkb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hkb, resolution 2.80&Aring;" /> '''CRYSTAL STRUCTURE O...)
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[[Image:1hkb.gif|left|200px]]<br />
 
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<applet load="1hkb" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1hkb, resolution 2.80&Aring;" />
 
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'''CRYSTAL STRUCTURE OF RECOMBINANT HUMAN BRAIN HEXOKINASE TYPE I COMPLEXED WITH GLUCOSE AND GLUCOSE-6-PHOSPHATE'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF RECOMBINANT HUMAN BRAIN HEXOKINASE TYPE I COMPLEXED WITH GLUCOSE AND GLUCOSE-6-PHOSPHATE==
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BACKGROUND: Hexokinase I is the pacemaker of glycolysis in brain tissue., The type I isozyme exhibits unique regulatory properties in that, physiological levels of phosphate relieve potent inhibition by the, product, glucose-6-phosphate (Gluc-6-P). The 100 kDa polypeptide chain of, hexokinase I consists of a C-terminal (catalytic) domain and an N-terminal, (regulatory) domain. Structures of ligated hexokinase I should provide a, basis for understanding mechanisms of catalysis and regulation at an, atomic level. RESULTS: The complex of human hexokinase I with glucose and, Gluc-6-P (determined to 2.8 A resolution) is a dimer with twofold, molecular symmetry. The N- and C-terminal domains of one monomer interact, with the C- and N-terminal domains, respectively, of the symmetry-related, ... [[http://ispc.weizmann.ac.il/pmbin/getpm?9493266 (full description)]]
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<StructureSection load='1hkb' size='340' side='right'caption='[[1hkb]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1hkb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HKB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HKB 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]] 2.8&#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=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=G6P:ALPHA-D-GLUCOSE-6-PHOSPHATE'>G6P</scene></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=1hkb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hkb OCA], [https://pdbe.org/1hkb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hkb RCSB], [https://www.ebi.ac.uk/pdbsum/1hkb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hkb ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/HXK1_HUMAN HXK1_HUMAN] Defects in HK1 are the cause of hexokinase deficiency (HK deficiency) [MIM:[https://omim.org/entry/235700 235700]. HK deficiency is a rare autosomal recessive disease with nonspherocytic hemolytic anemia as the predominant clinical feature.
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== Function ==
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[https://www.uniprot.org/uniprot/HXK1_HUMAN HXK1_HUMAN]
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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/hk/1hkb_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=1hkb 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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1HKB is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with GLC, G6P and CA as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.1 2.7.1.1]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HKB 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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The mechanism of regulation of hexokinase: new insights from the crystal structure of recombinant human brain hexokinase complexed with glucose and glucose-6-phosphate., Aleshin AE, Zeng C, Bourenkov GP, Bartunik HD, Fromm HJ, Honzatko RB, Structure. 1998 Jan 15;6(1):39-50. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9493266 9493266]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Aleshin, A.E.]]
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[[Category: Aleshin AE]]
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[[Category: Bartunik, H.D.]]
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[[Category: Bartunik HD]]
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[[Category: Burenkov, G.P.]]
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[[Category: Burenkov GP]]
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[[Category: Fromm, H.J.]]
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[[Category: Fromm HJ]]
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[[Category: Honzatko, R.B.]]
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[[Category: Honzatko RB]]
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[[Category: Zeng, C.]]
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[[Category: Zeng C]]
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[[Category: CA]]
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[[Category: G6P]]
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[[Category: GLC]]
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[[Category: allosteric enzyme]]
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[[Category: glucose]]
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[[Category: glucose-6-phosphate]]
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[[Category: glycolysis]]
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[[Category: phosphotransferase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 16:49:36 2007''
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Current revision

CRYSTAL STRUCTURE OF RECOMBINANT HUMAN BRAIN HEXOKINASE TYPE I COMPLEXED WITH GLUCOSE AND GLUCOSE-6-PHOSPHATE

PDB ID 1hkb

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