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| | <StructureSection load='2gz6' size='340' side='right'caption='[[2gz6]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='2gz6' size='340' side='right'caption='[[2gz6]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2gz6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Anabaena_sp._ch1 Anabaena sp. ch1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GZ6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2GZ6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2gz6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Anabaena_sp._CH1 Anabaena sp. CH1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GZ6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GZ6 FirstGlance]. <br> |
| - | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Mannose-6-phosphate_isomerase Mannose-6-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.8 5.3.1.8] </span></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]] 2Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2gz6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gz6 OCA], [http://pdbe.org/2gz6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2gz6 RCSB], [http://www.ebi.ac.uk/pdbsum/2gz6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2gz6 ProSAT]</span></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=2gz6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gz6 OCA], [https://pdbe.org/2gz6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gz6 RCSB], [https://www.ebi.ac.uk/pdbsum/2gz6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gz6 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A4UA16_9NOST A4UA16_9NOST] |
| | == 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: Anabaena sp. ch1]] | + | [[Category: Anabaena sp. CH1]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Mannose-6-phosphate isomerase]]
| + | [[Category: Chang YN]] |
| - | [[Category: Chang, Y N]] | + | [[Category: Wang WC]] |
| - | [[Category: Wang, W C]] | + | [[Category: Wu HM]] |
| - | [[Category: Wu, H M]] | + | |
| - | [[Category: Isomerase]]
| + | |
| - | [[Category: N-acetyl-d-glucosamine 2-epimerase]]
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| Structural highlights
Function
A4UA16_9NOST
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
N-acetyl-D-glucosamine 2-epimerase (GlcNAc 2-epimerase) catalyzes the reversible epimerization between N-acetyl-D-glucosamine (GlcNAc) and N-acetyl-D-mannosamine (ManNAc). We report here the 2.0 A resolution crystal structure of the GlcNAc 2-epimerase from Anabaena sp. CH1. The structure demonstrates an (alpha/alpha)(6) barrel fold, which shows structural homology with porcine GlcNAc 2-epimerase as well as a number of glycoside hydrolase enzymes and other sugar-metabolizing enzymes. One side of the barrel structure consists of short loops involved in dimer interactions. The other side of the barrel structure is comprised of long loops containing six short beta-sheets, which enclose a putative central active-site pocket. Site-directed mutagenesis of conserved residues near the N-terminal region of the inner alpha helices shows that R57, H239, E308, and H372 are strictly required for activity. E242 and R375 are also essential in catalysis. Based on the structure and kinetic analysis, H239 and H372 may serve as the key active site acid/base catalysts. These results suggest that the (alpha/alpha)(6) barrel represents a steady fold for presenting active-site residues in a cleft at the N-terminal ends of the inner alpha helices, thus forming a fine-tuned catalytic site in GlcNAc 2-epimerase.
The central cavity from the (alpha/alpha)6 barrel structure of Anabaena sp. CH1 N-acetyl-D-glucosamine 2-epimerase contains two key histidine residues for reversible conversion.,Lee YC, Wu HM, Chang YN, Wang WC, Hsu WH J Mol Biol. 2007 Mar 30;367(3):895-908. Epub 2006 Nov 6. PMID:17292397[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lee YC, Wu HM, Chang YN, Wang WC, Hsu WH. The central cavity from the (alpha/alpha)6 barrel structure of Anabaena sp. CH1 N-acetyl-D-glucosamine 2-epimerase contains two key histidine residues for reversible conversion. J Mol Biol. 2007 Mar 30;367(3):895-908. Epub 2006 Nov 6. PMID:17292397 doi:10.1016/j.jmb.2006.11.001
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