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1dlj
From Proteopedia
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|PDB= 1dlj |SIZE=350|CAPTION= <scene name='initialview01'>1dlj</scene>, resolution 1.80Å | |PDB= 1dlj |SIZE=350|CAPTION= <scene name='initialview01'>1dlj</scene>, resolution 1.80Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UGA:URIDINE-5'-DIPHOSPHATE-GLUCURONIC+ACID'>UGA</scene> |
| - | + | |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= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1dli|1DLI]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dlj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dlj OCA], [http://www.ebi.ac.uk/pdbsum/1dlj PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dlj RCSB]</span> | ||
}} | }} | ||
| Line 28: | Line 31: | ||
[[Category: Strynadka, N C.J.]] | [[Category: Strynadka, N C.J.]] | ||
[[Category: Tanner, M E.]] | [[Category: Tanner, M E.]] | ||
| - | [[Category: GOL]] | ||
| - | [[Category: NAI]] | ||
| - | [[Category: SO4]] | ||
| - | [[Category: UGA]] | ||
[[Category: crystallographic dimer]] | [[Category: crystallographic dimer]] | ||
[[Category: rossmann fold]] | [[Category: rossmann fold]] | ||
[[Category: ternary complex]] | [[Category: ternary complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:43:51 2008'' |
Revision as of 16:43, 30 March 2008
| |||||||
| , resolution 1.80Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Activity: | UDP-glucose 6-dehydrogenase, with EC number 1.1.1.22 | ||||||
| Related: | 1DLI
| ||||||
| 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
1DLJ 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
Page seeded by OCA on Sun Mar 30 19:43:51 2008
