This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1dlj
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1dlj.gif|left|200px]] | + | [[Image:1dlj.gif|left|200px]] |
| - | + | ||
| - | '''THE FIRST STRUCTURE OF UDP-GLUCOSE DEHYDROGENASE (UDPGDH) REVEALS THE CATALYTIC RESIDUES NECESSARY FOR THE TWO-FOLD OXIDATION''' | + | {{Structure |
| + | |PDB= 1dlj |SIZE=350|CAPTION= <scene name='initialview01'>1dlj</scene>, resolution 1.80Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</scene>, <scene name='pdbligand=UGA:URIDINE-5'-DIPHOSPHATE-GLUCURONIC+ACID'>UGA</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | ||
| + | |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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''THE FIRST STRUCTURE OF UDP-GLUCOSE DEHYDROGENASE (UDPGDH) REVEALS THE CATALYTIC RESIDUES NECESSARY FOR THE TWO-FOLD OXIDATION''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1DLJ is a [ | + | 1DLJ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_pyogenes Streptococcus pyogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DLJ OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10841783 10841783] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Streptococcus pyogenes]] | [[Category: Streptococcus pyogenes]] | ||
| Line 27: | Line 36: | ||
[[Category: ternary complex]] | [[Category: ternary complex]] | ||
| - | ''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 10:40:21 2008'' |
Revision as of 08:40, 20 March 2008
| |||||||
| , resolution 1.80Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , and | ||||||
| Activity: | UDP-glucose 6-dehydrogenase, with EC number 1.1.1.22 | ||||||
| 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 Thu Mar 20 10:40:21 2008
