2gz6
From Proteopedia
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| - | [[Image:2gz6.jpg|left|200px]] | + | [[Image:2gz6.jpg|left|200px]] |
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| - | '''Crystal Structure Of Anabaena sp. CH1 N-acetyl-D-glucosamine 2-epimerase At 2.0 A''' | + | {{Structure |
| + | |PDB= 2gz6 |SIZE=350|CAPTION= <scene name='initialview01'>2gz6</scene>, resolution 2.00Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Crystal Structure Of Anabaena sp. CH1 N-acetyl-D-glucosamine 2-epimerase At 2.0 A''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2GZ6 is a [ | + | 2GZ6 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Anabaena_sp. Anabaena sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GZ6 OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17292397 17292397] |
[[Category: Anabaena sp.]] | [[Category: Anabaena sp.]] | ||
[[Category: Mannose-6-phosphate isomerase]] | [[Category: Mannose-6-phosphate isomerase]] | ||
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[[Category: n-acetyl-d-glucosamine 2-epimerase]] | [[Category: n-acetyl-d-glucosamine 2-epimerase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:10:33 2008'' |
Revision as of 15:10, 20 March 2008
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| , resolution 2.00Å | |||||||
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| Activity: | Mannose-6-phosphate isomerase, with EC number 5.3.1.8 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure Of Anabaena sp. CH1 N-acetyl-D-glucosamine 2-epimerase At 2.0 A
Overview
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.
About this Structure
2GZ6 is a Protein complex structure of sequences from Anabaena sp.. Full crystallographic information is available from OCA.
Reference
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
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