2vhl
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:2vhl.jpg|left|200px]] | + | [[Image:2vhl.jpg|left|200px]] |
| - | + | ||
| - | '''THE THREE-DIMENSIONAL STRUCTURE OF THE N-ACETYLGLUCOSAMINE-6-PHOSPHATE DEACETYLASE FROM BACILLUS SUBTILIS''' | + | {{Structure |
| + | |PDB= 2vhl |SIZE=350|CAPTION= <scene name='initialview01'>2vhl</scene>, resolution 2.050Å | ||
| + | |SITE= <scene name='pdbsite=AC1:Glp+Binding+Site+For+Chain+A'>AC1</scene>, <scene name='pdbsite=AC2:Pig+Binding+Site+For+Chain+A'>AC2</scene>, <scene name='pdbsite=AC3:Fe+Binding+Site+For+Chain+A'>AC3</scene>, <scene name='pdbsite=AC4:Fe+Binding+Site+For+Chain+A'>AC4</scene>, <scene name='pdbsite=AC5:Glp+Binding+Site+For+Chain+B'>AC5</scene>, <scene name='pdbsite=AC6:Pig+Binding+Site+For+Chain+B'>AC6</scene>, <scene name='pdbsite=AC7:Fe+Binding+Site+For+Chain+B'>AC7</scene> and <scene name='pdbsite=AC8:Fe+Binding+Site+For+Chain+B'>AC8</scene> | ||
| + | |LIGAND= <scene name='pdbligand=GLP:GLUCOSAMINE+6-PHOSPHATE'>GLP</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene> and <scene name='pdbligand=PIG:2-[2-(2-HYDROXY-ETHOXY)-ETHOXY]-ETHANOL'>PIG</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/N-acetylglucosamine-6-phosphate_deacetylase N-acetylglucosamine-6-phosphate deacetylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.25 3.5.1.25] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''THE THREE-DIMENSIONAL STRUCTURE OF THE N-ACETYLGLUCOSAMINE-6-PHOSPHATE DEACETYLASE FROM BACILLUS SUBTILIS''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 2VHL is a [ | + | 2VHL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. This structure supersedes the now removed PDB entry 1UN7. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VHL OCA]. |
==Reference== | ==Reference== | ||
| - | The three-dimensional structure of the N-acetylglucosamine-6-phosphate deacetylase, NagA, from Bacillus subtilis: a member of the urease superfamily., Vincent F, Yates D, Garman E, Davies GJ, Brannigan JA, J Biol Chem. 2004 Jan 23;279(4):2809-16. Epub 2003 Oct 13. PMID:[http:// | + | The three-dimensional structure of the N-acetylglucosamine-6-phosphate deacetylase, NagA, from Bacillus subtilis: a member of the urease superfamily., Vincent F, Yates D, Garman E, Davies GJ, Brannigan JA, J Biol Chem. 2004 Jan 23;279(4):2809-16. Epub 2003 Oct 13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14557261 14557261] |
[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
[[Category: N-acetylglucosamine-6-phosphate deacetylase]] | [[Category: N-acetylglucosamine-6-phosphate deacetylase]] | ||
| Line 21: | Line 30: | ||
[[Category: GLP]] | [[Category: GLP]] | ||
[[Category: PIG]] | [[Category: PIG]] | ||
| - | [[Category: bacillus | + | [[Category: bacillus subtili]] |
[[Category: carbohydrate metabolism]] | [[Category: carbohydrate metabolism]] | ||
[[Category: deacetylase]] | [[Category: deacetylase]] | ||
| Line 27: | Line 36: | ||
[[Category: n- acetyleglucosamine-6-phosphate]] | [[Category: n- acetyleglucosamine-6-phosphate]] | ||
| - | ''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 18:46:39 2008'' |
Revision as of 16:46, 20 March 2008
| |||||||
| , resolution 2.050Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , , , , , and | ||||||
| Ligands: | , and | ||||||
| Activity: | N-acetylglucosamine-6-phosphate deacetylase, with EC number 3.5.1.25 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE THREE-DIMENSIONAL STRUCTURE OF THE N-ACETYLGLUCOSAMINE-6-PHOSPHATE DEACETYLASE FROM BACILLUS SUBTILIS
Overview
The enzyme N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl group of GlcNAc-6-P to yield glucosamine 6-phosphate and acetate, the first committed step in the biosynthetic pathway to amino-sugar-nucleotides. It is classified into carbohydrate esterase family CE-9 (see afmb.cnrs-mrs.fr/CAZY/). Here we report the cloning, expression, and three-dimensional structure (Protein Data Bank code 1un7) determination by x-ray crystallography of the Bacillus subtilis NagA at a resolution of 2.0 A. The structure presents two domains, a (beta/alpha)(8) barrel enclosing the active center and a small beta barrel domain. The structure is dimeric, and the substrate phosphate coordination at the active center is provided by an Arg/His pair contributed from the second molecule of the dimer. Both the overall structure and the active center bear a striking similarity to the urease superfamily with two metals involved in substrate binding and catalysis. PIXE (Proton-Induced x-ray Emission) data show that iron is the predominant metal in the purified protein. We propose a catalytic mechanism involving proton donation to the leaving group by aspartate, nucleophilic attack by an Fe-bridged hydroxide, and stabilization of the carbonyl oxygen by one of the two Fe atoms of the pair. We believe that this is the first sugar deacetylase to utilize this fold and catalytic mechanism.
About this Structure
2VHL is a Single protein structure of sequence from Bacillus subtilis. This structure supersedes the now removed PDB entry 1UN7. Full crystallographic information is available from OCA.
Reference
The three-dimensional structure of the N-acetylglucosamine-6-phosphate deacetylase, NagA, from Bacillus subtilis: a member of the urease superfamily., Vincent F, Yates D, Garman E, Davies GJ, Brannigan JA, J Biol Chem. 2004 Jan 23;279(4):2809-16. Epub 2003 Oct 13. PMID:14557261
Page seeded by OCA on Thu Mar 20 18:46:39 2008
