1dlj: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1dlj.gif|left|200px]] | [[Image:1dlj.gif|left|200px]] | ||
<!-- | |||
The line below this paragraph, containing "STRUCTURE_1dlj", creates the "Structure Box" on the page. | |||
You may change the PDB parameter (which sets the PDB file loaded into the applet) | |||
or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |||
or leave the SCENE parameter empty for the default display. | |||
| | --> | ||
| | {{STRUCTURE_1dlj| PDB=1dlj | SCENE= }} | ||
}} | |||
'''THE FIRST STRUCTURE OF UDP-GLUCOSE DEHYDROGENASE (UDPGDH) REVEALS THE CATALYTIC RESIDUES NECESSARY FOR THE TWO-FOLD OXIDATION''' | '''THE FIRST STRUCTURE OF UDP-GLUCOSE DEHYDROGENASE (UDPGDH) REVEALS THE CATALYTIC RESIDUES NECESSARY FOR THE TWO-FOLD OXIDATION''' | ||
| Line 31: | Line 28: | ||
[[Category: Strynadka, N C.J.]] | [[Category: Strynadka, N C.J.]] | ||
[[Category: Tanner, M E.]] | [[Category: Tanner, M E.]] | ||
[[Category: | [[Category: Crystallographic dimer]] | ||
[[Category: | [[Category: Rossmann fold]] | ||
[[Category: | [[Category: Ternary complex]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:59:15 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 10:59, 2 May 2008
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 Fri May 2 13:59:15 2008