1mmx: Difference between revisions

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New page: left|200px<br /><applet load="1mmx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mmx, resolution 1.80Å" /> '''Crystal structure of...
 
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[[Image:1mmx.gif|left|200px]]<br /><applet load="1mmx" size="450" color="white" frame="true" align="right" spinBox="true"
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'''Crystal structure of galactose mutarotase from Lactococcus lactis complexed with D-fucose'''<br />


==Overview==
==Crystal structure of galactose mutarotase from Lactococcus lactis complexed with D-fucose==
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.
<StructureSection load='1mmx' size='340' side='right'caption='[[1mmx]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1mmx]] 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=1MMX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MMX FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mmx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mmx OCA], [https://pdbe.org/1mmx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mmx RCSB], [https://www.ebi.ac.uk/pdbsum/1mmx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mmx ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9ZB17_9LACT Q9ZB17_9LACT]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mm/1mmx_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1mmx ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1MMX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Lactococcus_lactis Lactococcus lactis] with FUC and NA as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Aldose_1-epimerase Aldose 1-epimerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.1.3.3 5.1.3.3] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MMX OCA].
*[[Galactose mutarotase|Galactose mutarotase]]
 
__TOC__
==Reference==
</StructureSection>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=12218067 12218067]
[[Category: Aldose 1-epimerase]]
[[Category: Lactococcus lactis]]
[[Category: Lactococcus lactis]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Holden, H.M.]]
[[Category: Holden HM]]
[[Category: Kim, J.]]
[[Category: Kim J]]
[[Category: Raushel, F.M.]]
[[Category: Raushel FM]]
[[Category: Thoden, J.B.]]
[[Category: Thoden JB]]
[[Category: FUC]]
[[Category: NA]]
[[Category: epimerase]]
[[Category: galactosemia]]
[[Category: sugar binding]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 04:21:35 2007''

Latest revision as of 10:46, 14 February 2024

Crystal structure of galactose mutarotase from Lactococcus lactis complexed with D-fucoseCrystal structure of galactose mutarotase from Lactococcus lactis complexed with D-fucose

Structural highlights

1mmx is a 2 chain structure with sequence from Lactococcus lactis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.8Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q9ZB17_9LACT

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1mmx, resolution 1.80Å

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