1fxj
From Proteopedia
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| - | [[Image:1fxj.jpg|left|200px]] | + | [[Image:1fxj.jpg|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF N-ACETYLGLUCOSAMINE 1-PHOSPHATE URIDYLTRANSFERASE''' | + | {{Structure |
| + | |PDB= 1fxj |SIZE=350|CAPTION= <scene name='initialview01'>1fxj</scene>, resolution 2.25Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC ACID'>MES</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/UDP-N-acetylglucosamine_diphosphorylase UDP-N-acetylglucosamine diphosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.23 2.7.7.23] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF N-ACETYLGLUCOSAMINE 1-PHOSPHATE URIDYLTRANSFERASE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1FXJ is a [ | + | 1FXJ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FXJ OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure of the bifunctional N-acetylglucosamine 1-phosphate uridyltransferase from Escherichia coli: a paradigm for the related pyrophosphorylase superfamily., Brown K, Pompeo F, Dixon S, Mengin-Lecreulx D, Cambillau C, Bourne Y, EMBO J. 1999 Aug 2;18(15):4096-107. PMID:[http:// | + | Crystal structure of the bifunctional N-acetylglucosamine 1-phosphate uridyltransferase from Escherichia coli: a paradigm for the related pyrophosphorylase superfamily., Brown K, Pompeo F, Dixon S, Mengin-Lecreulx D, Cambillau C, Bourne Y, EMBO J. 1999 Aug 2;18(15):4096-107. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10428949 10428949] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: pyrophosphorylase]] | [[Category: pyrophosphorylase]] | ||
| - | ''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 11:15:22 2008'' |
Revision as of 09:15, 20 March 2008
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| , resolution 2.25Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Activity: | UDP-N-acetylglucosamine diphosphorylase, with EC number 2.7.7.23 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF N-ACETYLGLUCOSAMINE 1-PHOSPHATE URIDYLTRANSFERASE
Overview
N-acetylglucosamine 1-phosphate uridyltransferase (GlmU) is a cytoplasmic bifunctional enzyme involved in the biosynthesis of the nucleotide-activated UDP-GlcNAc, which is an essential precursor for the biosynthetic pathways of peptidoglycan and other components in bacteria. The crystal structure of a truncated form of GlmU has been solved at 2.25 A resolution using the multiwavelength anomalous dispersion technique and its function tested with mutagenesis studies. The molecule is composed of two distinct domains connected by a long alpha-helical arm: (i) an N-terminal domain which resembles the dinucleotide-binding Rossmann fold; and (ii) a C-terminal domain which adopts a left-handed parallel beta-helix structure (LbetaH) as found in homologous bacterial acetyltransferases. Three GlmU molecules assemble into a trimeric arrangement with tightly packed parallel LbetaH domains, the long alpha-helical linkers being seated on top of the arrangement and the N-terminal domains projected away from the 3-fold axis. In addition, the 2.3 A resolution structure of the GlmU-UDP-GlcNAc complex reveals the structural bases required for the uridyltransferase activity. These structures exemplify a three-dimensional template for the development of new antibacterial agents and for studying other members of the large family of XDP-sugar bacterial pyrophosphorylases.
About this Structure
1FXJ is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Crystal structure of the bifunctional N-acetylglucosamine 1-phosphate uridyltransferase from Escherichia coli: a paradigm for the related pyrophosphorylase superfamily., Brown K, Pompeo F, Dixon S, Mengin-Lecreulx D, Cambillau C, Bourne Y, EMBO J. 1999 Aug 2;18(15):4096-107. PMID:10428949
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