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| | <StructureSection load='1so0' size='340' side='right'caption='[[1so0]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='1so0' size='340' side='right'caption='[[1so0]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1so0]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SO0 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1SO0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1so0]] is a 4 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=1SO0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SO0 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1snz|1snz]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GALM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=1so0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1so0 OCA], [https://pdbe.org/1so0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1so0 RCSB], [https://www.ebi.ac.uk/pdbsum/1so0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1so0 ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1so0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1so0 OCA], [http://pdbe.org/1so0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1so0 RCSB], [http://www.ebi.ac.uk/pdbsum/1so0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1so0 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/GALM_HUMAN GALM_HUMAN]] Mutarotase converts alpha-aldose to the beta-anomer. It is active on D-glucose, L-arabinose, D-xylose, D-galactose, maltose and lactose (By similarity).<ref>PMID:12753898</ref> <ref>PMID:15026423</ref> | + | [https://www.uniprot.org/uniprot/GALM_HUMAN GALM_HUMAN] Mutarotase converts alpha-aldose to the beta-anomer. It is active on D-glucose, L-arabinose, D-xylose, D-galactose, maltose and lactose (By similarity).<ref>PMID:12753898</ref> <ref>PMID:15026423</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Aldose 1-epimerase]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Human]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Holden, H M]] | + | [[Category: Holden HM]] |
| - | [[Category: Reece, R J]] | + | [[Category: Reece RJ]] |
| - | [[Category: Thoden, J B]] | + | [[Category: Thoden JB]] |
| - | [[Category: Timson, D J]] | + | [[Category: Timson DJ]] |
| - | [[Category: Epimerase]]
| + | |
| - | [[Category: Galactosemia]]
| + | |
| - | [[Category: Isomerase]]
| + | |
| - | [[Category: Mutartoase]]
| + | |
| Structural highlights
Function
GALM_HUMAN Mutarotase converts alpha-aldose to the beta-anomer. It is active on D-glucose, L-arabinose, D-xylose, D-galactose, maltose and lactose (By similarity).[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Galactose mutarotase catalyzes the conversion of beta-d-galactose to alpha-d-galactose during normal galactose metabolism. The enzyme has been isolated from bacteria, plants, and animals and is present in the cytoplasm of most cells. Here we report the x-ray crystallographic analysis of human galactose mutarotase both in the apoform and complexed with its substrate, beta-d-galactose. The polypeptide chain folds into an intricate array of 29 beta-strands, 25 classical reverse turns, and 2 small alpha-helices. There are two cis-peptide bonds at Arg-78 and Pro-103. The sugar ligand sits in a shallow cleft and is surrounded by Asn-81, Arg-82, His-107, His-176, Asp-243, Gln-279, and Glu-307. Both the side chains of Glu-307 and His-176 are in the proper location to act as a catalytic base and a catalytic acid, respectively. These residues are absolutely conserved among galactose mutarotases. To date, x-ray models for three mutarotases have now been reported, namely that described here and those from Lactococcus lactis and Caenorhabditis elegans. The molecular architectures of these enzymes differ primarily in the loop regions connecting the first two beta-strands. In the human protein, there are six extra residues in the loop compared with the bacterial protein for an approximate longer length of 9 A. In the C. elegans protein, the first 17 residues are missing, thereby reducing the total number of beta-strands by one.
Molecular structure of human galactose mutarotase.,Thoden JB, Timson DJ, Reece RJ, Holden HM J Biol Chem. 2004 May 28;279(22):23431-7. Epub 2004 Mar 16. PMID:15026423[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Timson DJ, Reece RJ. Identification and characterisation of human aldose 1-epimerase. FEBS Lett. 2003 May 22;543(1-3):21-4. PMID:12753898
- ↑ Thoden JB, Timson DJ, Reece RJ, Holden HM. Molecular structure of human galactose mutarotase. J Biol Chem. 2004 May 28;279(22):23431-7. Epub 2004 Mar 16. PMID:15026423 doi:10.1074/jbc.M402347200
- ↑ Thoden JB, Timson DJ, Reece RJ, Holden HM. Molecular structure of human galactose mutarotase. J Biol Chem. 2004 May 28;279(22):23431-7. Epub 2004 Mar 16. PMID:15026423 doi:10.1074/jbc.M402347200
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