2uuv

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|PDB= 2uuv |SIZE=350|CAPTION= <scene name='initialview01'>2uuv</scene>, resolution 1.99&Aring;
|PDB= 2uuv |SIZE=350|CAPTION= <scene name='initialview01'>2uuv</scene>, resolution 1.99&Aring;
|SITE= <scene name='pdbsite=AC1:Pl3+Binding+Site+For+Chain+D'>AC1</scene>
|SITE= <scene name='pdbsite=AC1:Pl3+Binding+Site+For+Chain+D'>AC1</scene>
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|LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene> and <scene name='pdbligand=PL3:HEXADECAN-1-OL'>PL3</scene>
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|LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=PL3:HEXADECAN-1-OL'>PL3</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Alkylglycerone-phosphate_synthase Alkylglycerone-phosphate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.26 2.5.1.26]
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Alkylglycerone-phosphate_synthase Alkylglycerone-phosphate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.26 2.5.1.26] </span>
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2uuv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2uuv OCA], [http://www.ebi.ac.uk/pdbsum/2uuv PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2uuv RCSB]</span>
}}
}}
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[[Category: Pandini, V.]]
[[Category: Pandini, V.]]
[[Category: Razeto, A.]]
[[Category: Razeto, A.]]
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[[Category: FAD]]
 
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[[Category: PL3]]
 
[[Category: biosynthesis of phospholipid]]
[[Category: biosynthesis of phospholipid]]
[[Category: fad]]
[[Category: fad]]
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[[Category: transferase]]
[[Category: transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:40:03 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:04:49 2008''

Revision as of 02:04, 31 March 2008


PDB ID 2uuv

Drag the structure with the mouse to rotate
, resolution 1.99Å
Sites:
Ligands: ,
Activity: Alkylglycerone-phosphate synthase, with EC number 2.5.1.26
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



ALKYLDIHYDROXYACETONEPHOSPHATE SYNTHASE IN P1


Overview

Ether phospholipids are essential constituents of eukaryotic cell membranes. Rhizomelic chondrodysplasia punctata type 3 is a severe peroxisomal disorder caused by inborn deficiency of alkyldihydroxyacetonephosphate synthase (ADPS). The enzyme carries out the most characteristic step in ether phospholipid biosynthesis: formation of the ether bond. The crystal structure of ADPS from Dictyostelium discoideum shows a fatty-alcohol molecule bound in a narrow hydrophobic tunnel, specific for aliphatic chains of 16 carbons. Access to the tunnel is controlled by a flexible loop and a gating helix at the protein-membrane interface. Structural and mutagenesis investigations identify a cluster of hydrophilic catalytic residues, including an essential tyrosine, possibly involved in substrate proton abstraction, and the arginine that is mutated in ADPS-deficient patients. We propose that ether bond formation might be orchestrated through a covalent imine intermediate with the flavin, accounting for the noncanonical employment of a flavin cofactor in a nonredox reaction.

About this Structure

2UUV is a Single protein structure of sequence from Dictyostelium discoideum. Full crystallographic information is available from OCA.

Reference

The crucial step in ether phospholipid biosynthesis: structural basis of a noncanonical reaction associated with a peroxisomal disorder., Razeto A, Mattiroli F, Carpanelli E, Aliverti A, Pandini V, Coda A, Mattevi A, Structure. 2007 Jun;15(6):683-92. PMID:17562315

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