1dli

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|PDB= 1dli |SIZE=350|CAPTION= <scene name='initialview01'>1dli</scene>, resolution 2.31&Aring;
|PDB= 1dli |SIZE=350|CAPTION= <scene name='initialview01'>1dli</scene>, resolution 2.31&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=UDX:URIDINE-5&#39;-DIPHOSPHATE-XYLOPYRANOSE'>UDX</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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|LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UDX:URIDINE-5&#39;-DIPHOSPHATE-XYLOPYRANOSE'>UDX</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/UDP-glucose_6-dehydrogenase UDP-glucose 6-dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.22 1.1.1.22]
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/UDP-glucose_6-dehydrogenase UDP-glucose 6-dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.22 1.1.1.22] </span>
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=[[1dlj|1DLJ]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dli FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dli OCA], [http://www.ebi.ac.uk/pdbsum/1dli PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dli RCSB]</span>
}}
}}
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[[Category: Strynadka, N C.J.]]
[[Category: Strynadka, N C.J.]]
[[Category: Tanner, M E.]]
[[Category: Tanner, M E.]]
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[[Category: GOL]]
 
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[[Category: NAD]]
 
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[[Category: SO4]]
 
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[[Category: UDX]]
 
[[Category: crystallographic dimer]]
[[Category: crystallographic dimer]]
[[Category: rossmann fold]]
[[Category: rossmann fold]]
[[Category: ternary complex]]
[[Category: ternary complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 11:31:41 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:43:53 2008''

Revision as of 16:43, 30 March 2008


PDB ID 1dli

Drag the structure with the mouse to rotate
, resolution 2.31Å
Ligands: , , ,
Activity: UDP-glucose 6-dehydrogenase, with EC number 1.1.1.22
Related: 1DLJ


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



THE FIRST STRUCTURE OF UDP-GLUCOSE DEHYDROGENASE (UDPGDH) REVEALS THE CATALYTIC RESIDUES NECESSARY FOR THE TWO-FOLD OXIDATION


Overview

Bacterial UDP-glucose dehydrogenase (UDPGlcDH) is essential for formation of the antiphagocytic capsule that protects many virulent bacteria such as Streptococcus pyogenes andStreptococcus pneumoniae type 3 from the host's immune system. We have determined the X-ray structures of both native and Cys260Ser UDPGlcDH from S. pyogenes (74% similarity to S. pneumoniae) in ternary complexes with UDP-xylose/NAD(+) and UDP-glucuronic acid/NAD(H), respectively. The 402 residue homodimeric UDPGlcDH is composed of an N-terminal NAD(+) dinucleotide binding domain and a C-terminal UDP-sugar binding domain connected by a long (48 A) central alpha-helix. The first 290 residues of UDPGlcDH share structural homology with 6-phosphogluconate dehydrogenase, including conservation of an active site lysine and asparagine that are implicated in the enzyme mechanism. Also proposed to participate in the catalytic mechanism are a threonine and a glutamate that hydrogen bond to a conserved active site water molecule suitably positioned for general acid/base catalysis.

About this Structure

1DLI is a Single protein structure of sequence from Streptococcus pyogenes. Full crystallographic information is available from OCA.

Reference

The first structure of UDP-glucose dehydrogenase reveals the catalytic residues necessary for the two-fold oxidation., Campbell RE, Mosimann SC, van De Rijn I, Tanner ME, Strynadka NC, Biochemistry. 2000 Jun 13;39(23):7012-23. PMID:10841783

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