2bln
From Proteopedia
(New page: 200px<br /> <applet load="2bln" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bln, resolution 1.20Å" /> '''N-TERMINAL FORMYLTR...) |
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==About this Structure== | ==About this Structure== | ||
| - | 2BLN is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]] with ACT, FON and U5P as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.2 2.1.1.2]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BLN OCA]]. | + | 2BLN is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]] with ACT, FON and U5P as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Guanidinoacetate_N-methyltransferase Guanidinoacetate N-methyltransferase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.2 2.1.1.2]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BLN OCA]]. |
==Reference== | ==Reference== | ||
Structure and function of both domains of ArnA, a dual function decarboxylase and a formyltransferase, involved in 4-amino-4-deoxy-L-arabinose biosynthesis., Williams GJ, Breazeale SD, Raetz CR, Naismith JH, J Biol Chem. 2005 Jun 17;280(24):23000-8. Epub 2005 Apr 4. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15809294 15809294] | Structure and function of both domains of ArnA, a dual function decarboxylase and a formyltransferase, involved in 4-amino-4-deoxy-L-arabinose biosynthesis., Williams GJ, Breazeale SD, Raetz CR, Naismith JH, J Biol Chem. 2005 Jun 17;280(24):23000-8. Epub 2005 Apr 4. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15809294 15809294] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
| + | [[Category: Guanidinoacetate N-methyltransferase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Breazeale, S.D.]] | [[Category: Breazeale, S.D.]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 13:52:18 2007'' |
Revision as of 11:47, 30 October 2007
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N-TERMINAL FORMYLTRANSFERASE DOMAIN OF ARNA IN COMPLEX WITH N-5-FORMYLTETRAHYDROFOLATE AND UMP
Overview
Modification of the lipid A moiety of lipopolysaccharide by the addition, of the sugar 4-amino-4-deoxy-L-arabinose (L-Ara4N) is a strategy adopted, by pathogenic Gram-negative bacteria to evade cationic antimicrobial, peptides produced by the innate immune system. L-Ara4N biosynthesis is, therefore a potential anti-infective target, because inhibiting its, synthesis would render certain pathogens more sensitive to the immune, system. The bifunctional enzyme ArnA, which is required for L-Ara4N, biosynthesis, catalyzes the NAD(+)-dependent oxidative decarboxylation of, UDP-glucuronic acid to generate a UDP-4'-keto-pentose sugar and also, catalyzes transfer of a formyl group from N-10-formyltetrahydrofolate to, the 4'-amine of UDP-L-Ara4N. We now report the crystal structure of the, ... [(full description)]
About this Structure
2BLN is a [Single protein] structure of sequence from [Escherichia coli] with ACT, FON and U5P as [ligands]. Active as [Guanidinoacetate N-methyltransferase], with EC number [2.1.1.2]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Structure and function of both domains of ArnA, a dual function decarboxylase and a formyltransferase, involved in 4-amino-4-deoxy-L-arabinose biosynthesis., Williams GJ, Breazeale SD, Raetz CR, Naismith JH, J Biol Chem. 2005 Jun 17;280(24):23000-8. Epub 2005 Apr 4. PMID:15809294
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