3bn1
From Proteopedia
(New page: 200px {{Structure |PDB= 3bn1 |SIZE=350|CAPTION= <scene name='initialview01'>3bn1</scene>, resolution 1.8Å |SITE= <scene name='pdbsite=AC1:Act+Binding+Site+F...) |
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|PDB= 3bn1 |SIZE=350|CAPTION= <scene name='initialview01'>3bn1</scene>, resolution 1.8Å | |PDB= 3bn1 |SIZE=350|CAPTION= <scene name='initialview01'>3bn1</scene>, resolution 1.8Å | ||
|SITE= <scene name='pdbsite=AC1:Act+Binding+Site+For+Residue+A+372'>AC1</scene>, <scene name='pdbsite=AC2:Act+Binding+Site+For+Residue+C+372'>AC2</scene>, <scene name='pdbsite=AC3:Act+Binding+Site+For+Residue+D+372'>AC3</scene>, <scene name='pdbsite=AC4:Na+Binding+Site+For+Residue+A+373'>AC4</scene> and <scene name='pdbsite=AC5:Akg+Binding+Site+For+Residue+A+374'>AC5</scene> | |SITE= <scene name='pdbsite=AC1:Act+Binding+Site+For+Residue+A+372'>AC1</scene>, <scene name='pdbsite=AC2:Act+Binding+Site+For+Residue+C+372'>AC2</scene>, <scene name='pdbsite=AC3:Act+Binding+Site+For+Residue+D+372'>AC3</scene>, <scene name='pdbsite=AC4:Na+Binding+Site+For+Residue+A+373'>AC4</scene> and <scene name='pdbsite=AC5:Akg+Binding+Site+For+Residue+A+374'>AC5</scene> | ||
| - | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=AKG:2-OXYGLUTARIC+ACID'>AKG</scene>, <scene name='pdbligand=IT1:(E)-N~6~-({3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)METHYL]PYRIDIN-4-YL}METHYLIDENE)-L-LYSINE'>IT1</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= Per ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=155892 Caulobacter vibrioides]) | |GENE= Per ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=155892 Caulobacter vibrioides]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3bn1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bn1 OCA], [http://www.ebi.ac.uk/pdbsum/3bn1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3bn1 RCSB]</span> | ||
}} | }} | ||
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[[Category: Cook, P D.]] | [[Category: Cook, P D.]] | ||
[[Category: Holden, H M.]] | [[Category: Holden, H M.]] | ||
| - | [[Category: ACT]] | ||
| - | [[Category: AKG]] | ||
| - | [[Category: NA]] | ||
[[Category: aspartate aminotransferase]] | [[Category: aspartate aminotransferase]] | ||
[[Category: deoxysugar]] | [[Category: deoxysugar]] | ||
| Line 33: | Line 33: | ||
[[Category: x-ray structure]] | [[Category: x-ray structure]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:27:32 2008'' |
Revision as of 02:27, 31 March 2008
| |||||||
| , resolution 1.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , , and | ||||||
| Ligands: | , , , | ||||||
| Gene: | Per (Caulobacter vibrioides) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of GDP-perosamine synthase
Overview
Perosamine or 4-amino-4,6-dideoxy- d-mannose is an unusual sugar found in the O-antigens of some Gram-negative bacteria such as Vibrio cholerae O1 (the causative agent of cholera) or Escherichia coli O157:H7 (the leading cause of food-borne illnesses). It and similar deoxysugars are added to the O-antigens of bacteria via the action of glycosyltransferases that employ nucleotide-linked sugars as their substrates. The focus of this report is GDP-perosamine synthase, a PLP-dependent enzyme that catalyzes the last step in the formation of GDP-perosamine, namely, the amination of the sugar C-4'. Here we describe the three-dimensional structure of the enzyme from Caulobacter crescentus determined to a nominal resolution of 1.8 A and refined to an R-factor of 17.9%. The overall fold of the enzyme places it into the well-characterized aspartate aminotransferase superfamily. Each subunit of the dimeric enzyme contains a seven-stranded mixed beta-sheet, a two-stranded antiparallel beta-sheet, and 12 alpha-helices. Amino acid residues from both subunits form the active sites of the GDP-perosamine synthase dimer. Recently, the structure of another PLP-dependent enzyme, GDP-4-keto-6-deoxy- d-mannose-3-dehydratase (or ColD), was determined in our laboratory, and this enzyme employs the same substrate as GDP-perosamine synthase. Unlike GDP-perosamine synthase, however, ColD functions as a dehydratase that removes the sugar C-3' hydroxyl group. By purifying the ColD product and reacting it with purified GDP-perosamine synthase, we have produced a novel GDP-linked sugar, GDP-4-amino-3,4,6-trideoxy- d-mannose. Details describing the X-ray structural investigation of GDP-perosamine synthase and the enzymatic synthesis of GDP-4-amino-3,4,6-trideoxy- d-mannose are presented.
About this Structure
3BN1 is a Single protein structure of sequence from Caulobacter vibrioides. Full crystallographic information is available from OCA.
Reference
GDP-Perosamine Synthase: Structural Analysis and Production of a Novel Trideoxysugar(,)., Cook PD, Holden HM, Biochemistry. 2008 Mar 4;47(9):2833-40. Epub 2008 Feb 5. PMID:18247575
Page seeded by OCA on Mon Mar 31 05:27:32 2008
