1mn0

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[[Image:1mn0.jpg|left|200px]]
 
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==Crystal structure of galactose mutarotase from lactococcus lactis complexed with D-xylose==
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The line below this paragraph, containing "STRUCTURE_1mn0", creates the "Structure Box" on the page.
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<StructureSection load='1mn0' size='340' side='right'caption='[[1mn0]], [[Resolution|resolution]] 1.90&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'>[[1mn0]] is a 2 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=1MN0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MN0 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]] 1.9&#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=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=XYS:XYLOPYRANOSE'>XYS</scene></td></tr>
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{{STRUCTURE_1mn0| PDB=1mn0 | 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=1mn0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mn0 OCA], [https://pdbe.org/1mn0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mn0 RCSB], [https://www.ebi.ac.uk/pdbsum/1mn0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mn0 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q9ZB17_9LACT Q9ZB17_9LACT]
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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/mn/1mn0_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=1mn0 ConSurf].
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<div style="clear:both"></div>
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'''Crystal structure of galactose mutarotase from lactococcus lactis complexed with D-xylose'''
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==See Also==
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*[[Galactose mutarotase|Galactose mutarotase]]
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__TOC__
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==Overview==
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</StructureSection>
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Galactose mutarotase catalyzes the conversion of beta-D-galactose to alpha-D-galactose in the Leloir pathway for galactose metabolism. The high resolution x-ray structure of the dimeric enzyme from Lactococcus lactis was recently solved and shown to be topologically similar to the 18-stranded, anti-parallel beta-motif observed for domain 5 of beta-galactosidase. In addition to determining the overall molecular fold of galactose mutarotase, this initial investigation also provided a detailed description of the electrostatic interactions between the enzyme and its physiologically relevant substrate, galactose. Specifically, the side chains of His-96 and His-170 were shown to be located within hydrogen bonding distance to the C-5 oxygen of the substrate, while the carboxylate of Glu-304 was positioned near the C-1 hydroxyl group of the sugar. On the basis of this initial study, a possible role for Glu-304 as the general acid/base group in catalysis was put forth. Here we describe the combined x-ray crystallographic and kinetic analyses of L. lactis galactose mutarotase complexed with D-glucose, D-fucose, D-quinovose, L-arabinose, or D-xylose. These investigations have revealed that there are several distinct binding modes for these sugars, which are dependent upon the spatial orientation of the C-4 hydroxyl group. In those sugars with the same C-4 hydroxyl group orientation as galactose, their C-1 hydroxyl groups are invariably located near Glu-304. For those sugars, which have the same C-4 hydroxyl group configuration as glucose, the C-1 hydroxyls are typically located near Asp-243. These different binding modes correlate with both the observed kinetic parameters and the presence or absence of a hydrogen bond between the guanidinium group of Arg-71 and the C-4 hydroxyl group of the sugar ligand.
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==About this Structure==
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1MN0 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=1MN0 OCA].
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==Reference==
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Structural and kinetic studies of sugar binding to galactose mutarotase from Lactococcus lactis., Thoden JB, Kim J, Raushel FM, Holden HM, J Biol Chem. 2002 Nov 22;277(47):45458-65. Epub 2002 Sep 5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12218067 12218067]
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[[Category: Aldose 1-epimerase]]
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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: Kim, J.]]
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[[Category: Kim J]]
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[[Category: Raushel, F M.]]
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[[Category: Raushel FM]]
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[[Category: Thoden, J B.]]
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[[Category: Thoden JB]]
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[[Category: Epimerase]]
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[[Category: Galactosemia]]
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[[Category: Sugar binding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:26:23 2008''
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Current revision

Crystal structure of galactose mutarotase from lactococcus lactis complexed with D-xylose

PDB ID 1mn0

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