2a2c

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(New page: 200px<br /> <applet load="2a2c" size="450" color="white" frame="true" align="right" spinBox="true" caption="2a2c, resolution 1.65&Aring;" /> '''x-ray structure of ...)
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[[Image:2a2c.gif|left|200px]]<br />
 
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<applet load="2a2c" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2a2c, resolution 1.65&Aring;" />
 
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'''x-ray structure of human N-acetyl galactosamine kinase complexed with Mg-ADP and N-acetyl galactosamine 1-phosphate'''<br />
 
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==Overview==
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==x-ray structure of human N-acetyl galactosamine kinase complexed with Mg-ADP and N-acetyl galactosamine 1-phosphate==
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Galactokinase plays a key role in normal galactose metabolism by, catalyzing the conversion of alpha-d-galactose to galactose 1-phosphate., Within recent years, the three-dimensional structures of human, galactokinase and two bacterial forms of the enzyme have been determined., Originally, the gene encoding galactokinase in humans was mapped to, chromosome 17. An additional gene, encoding a protein with sequence, similarity to galactokinase, was subsequently mapped to chromosome 15., Recent reports have shown that this second gene (GALK2) encodes an enzyme, with greater activity against GalNAc than galactose. This enzyme, GalNAc, kinase, has been implicated in a salvage pathway for the reutilization of, free GalNAc derived from the degradation of complex carbohydrates. Here we, report the first structural analysis of a GalNAc kinase. The structure of, the human enzyme was solved in the presence of MnAMPPNP and GalNAc or, MgATP and GalNAc (which resulted in bound products in the active site)., The enzyme displays a distinctly bilobal appearance with its active site, wedged between the two domains. The N-terminal region is dominated by a, seven-stranded mixed beta-sheet, whereas the C-terminal motif contains two, layers of anti-parallel beta-sheet. The overall topology displayed by, GalNAc kinase places it into the GHMP superfamily of enzymes, which, generally function as small molecule kinases. From this investigation, the, geometry of the GalNAc kinase active site before and after catalysis has, been revealed, and the determinants of substrate specificity have been, defined on a molecular level.
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<StructureSection load='2a2c' size='340' side='right'caption='[[2a2c]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2a2c]] is a 1 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=2A2C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2A2C 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]] 1.65&#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=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NG1:N-ACETYL-ALPHA-D-GALACTOSAMINE+1-PHOSPHATE'>NG1</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=2a2c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a2c OCA], [https://pdbe.org/2a2c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2a2c RCSB], [https://www.ebi.ac.uk/pdbsum/2a2c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2a2c ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GALK2_HUMAN GALK2_HUMAN] Acts on GalNAc. Also acts as a galactokinase when galactose is present at high concentrations. May be involved in a salvage pathway for the reutilization of free GalNAc derived from the degradation of complex carbohydrates.<ref>PMID:8798585</ref> <ref>PMID:16006554</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/a2/2a2c_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=2a2c 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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2A2C 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 NG1, MG, CL, NA and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2A2C OCA].
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*[[Cyclophilin 3D structures|Cyclophilin 3D structures]]
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== References ==
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==Reference==
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<references/>
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The molecular architecture of human N-acetylgalactosamine kinase., Thoden JB, Holden HM, J Biol Chem. 2005 Sep 23;280(38):32784-91. Epub 2005 Jul 8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16006554 16006554]
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__TOC__
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</StructureSection>
[[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: 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: ADP]]
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[[Category: CL]]
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[[Category: MG]]
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[[Category: NA]]
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[[Category: NG1]]
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[[Category: galactokinase]]
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[[Category: kinase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:45:09 2007''
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Current revision

x-ray structure of human N-acetyl galactosamine kinase complexed with Mg-ADP and N-acetyl galactosamine 1-phosphate

PDB ID 2a2c

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