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1pie

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[[Image:1pie.gif|left|200px]]
 
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{{Structure
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==Crystal Structure of Lactococcus lactis Galactokinase Complexed with Galactose==
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|PDB= 1pie |SIZE=350|CAPTION= <scene name='initialview01'>1pie</scene>, resolution 2.10&Aring;
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<StructureSection load='1pie' size='340' side='right'caption='[[1pie]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=GLA:ALPHA+D-GALACTOSE'>GLA</scene> and <scene name='pdbligand=PO4:PHOSPHATE ION'>PO4</scene>
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<table><tr><td colspan='2'>[[1pie]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lactococcus_lactis Lactococcus lactis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PIE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PIE FirstGlance]. <br>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Galactokinase Galactokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.6 2.7.1.6]
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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]] 2.1&#8491;</td></tr>
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|GENE= GALK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1358 Lactococcus lactis])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLA:ALPHA+D-GALACTOSE'>GLA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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}}
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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=1pie FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pie OCA], [https://pdbe.org/1pie PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pie RCSB], [https://www.ebi.ac.uk/pdbsum/1pie PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pie ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GAL1_LACLA GAL1_LACLA] Catalyzes the transfer of the gamma-phosphate of ATP to D-galactose to form alpha-D-galactose-1-phosphate (Gal-1-P) (Probable).<ref>PMID:12796487</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/pi/1pie_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=1pie ConSurf].
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<div style="clear:both"></div>
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'''Crystal Structure of Lactococcus lactis Galactokinase Complexed with Galactose'''
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==See Also==
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*[[Galactokinase|Galactokinase]]
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== References ==
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==Overview==
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<references/>
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Galactokinase plays a key role in normal galactose metabolism by catalyzing the ATP-dependent phosphorylation of alpha-D-galactose to galactose 1-phosphate. In humans, mutations in the galactokinase gene can lead to the diseased state referred to as Type II galactosemia. Here we describe the three-dimensional structure of galactokinase from Lactococcus lactis determined to 2.1-A resolution. As expected from amino acid sequence alignments, galactokinase adopts a similar topology to that observed for members of the GHMP superfamily. The N-terminal domain is characterized by a five-stranded mixed beta-sheet while the C-terminal motif is dominated by two distinct four-stranded anti-parallel beta-sheets. The structure was solved in the presence of alpha-D-galactose and inorganic phosphate. These ligands are wedged between the N- and C-terminal domains. Amino acid side chains responsible for anchoring the sugar ligand to the protein include Arg36, Glu42, Asp45, Asp183, and Tyr233. Both Arg36 and Asp183 are strictly conserved in the amino acid sequences available in the literature thus far for galactokinases. Interestingly, the carboxylate side chain of Asp183 is positioned within 3.5 A of the C-1 hydroxyl group of galactose, whereas the guanidinium group of Arg36 is situated between both the C-1 hydroxyl group and the inorganic phosphate. Most likely these residues play key roles in catalysis. The structure of galactokinase described here serves as a model for understanding the functional consequences of point mutations known to result in Type II galactosemia in humans.
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__TOC__
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</StructureSection>
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==About this Structure==
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1PIE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Lactococcus_lactis Lactococcus lactis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PIE OCA].
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==Reference==
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Molecular structure of galactokinase., Thoden JB, Holden HM, J Biol Chem. 2003 Aug 29;278(35):33305-11. Epub 2003 Jun 9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12796487 12796487]
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[[Category: Galactokinase]]
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[[Category: Lactococcus lactis]]
[[Category: Lactococcus lactis]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Holden, H M.]]
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[[Category: Holden HM]]
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[[Category: Thoden, J B.]]
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[[Category: Thoden JB]]
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[[Category: GLA]]
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[[Category: PO4]]
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[[Category: galactose]]
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[[Category: galactosemia]]
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[[Category: kinase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:24:41 2008''
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Current revision

Crystal Structure of Lactococcus lactis Galactokinase Complexed with Galactose

PDB ID 1pie

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