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| - | [[Image:1un7.gif|left|200px]]<br /> | + | [[Image:1un7.gif|left|200px]]<br /><applet load="1un7" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1un7" size="450" color="white" frame="true" align="right" spinBox="true" | + | caption="1un7" /> |
| - | caption="1un7, resolution 2.05Å" /> | + | ''''''<br /> |
| - | '''THE 3-D STRUCTURE OF THE N-ACETYLGLUCOSAMINE-6-PHOSPHATE DEACETYLASE, NAGA, FROM BACILLUS SUBTILIS: A MEMBER OF THE UREASE SUPERFAMILY'''<br /> | + | |
| - | | + | |
| - | ==Overview==
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| - | 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.
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| | ==About this Structure== | | ==About this Structure== |
| - | 1UN7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with GLP, FE and 2PE as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UN7 OCA].
| + | is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id= OCA]. |
| - | | + | [[Category: Protein complex]] |
| - | ==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://ispc.weizmann.ac.il//pmbin/getpm?pmid=14557261 14557261]
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| - | [[Category: Bacillus subtilis]] | + | |
| - | [[Category: N-acetylglucosamine-6-phosphate deacetylase]]
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| - | [[Category: Single protein]]
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| - | [[Category: Brannigan, J.A.]]
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| - | [[Category: Davies, G.J.]]
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| - | [[Category: Garman, E.]]
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| - | [[Category: Vincent, F.]]
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| - | [[Category: Yates, D.]]
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| - | [[Category: 2PE]]
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| - | [[Category: FE]]
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| - | [[Category: GLP]]
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| - | [[Category: bacillus subtilis]]
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| - | [[Category: deacetylase ]]
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| - | [[Category: hydrolase]]
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| - | [[Category: n-acetyleglucosamine-6-phosphate]]
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| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 17:06:57 2007'' | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 18:04:02 2007'' |
