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1dlj
From Proteopedia
(New page: 200px<br /><applet load="1dlj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dlj, resolution 1.80Å" /> '''THE FIRST STRUCTURE ...) |
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| - | [[Image:1dlj.gif|left|200px]]<br /><applet load="1dlj" size=" | + | [[Image:1dlj.gif|left|200px]]<br /><applet load="1dlj" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1dlj, resolution 1.80Å" /> | caption="1dlj, resolution 1.80Å" /> | ||
'''THE FIRST STRUCTURE OF UDP-GLUCOSE DEHYDROGENASE (UDPGDH) REVEALS THE CATALYTIC RESIDUES NECESSARY FOR THE TWO-FOLD OXIDATION'''<br /> | '''THE FIRST STRUCTURE OF UDP-GLUCOSE DEHYDROGENASE (UDPGDH) REVEALS THE CATALYTIC RESIDUES NECESSARY FOR THE TWO-FOLD OXIDATION'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Bacterial UDP-glucose dehydrogenase (UDPGlcDH) is essential for formation | + | 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== | ==About this Structure== | ||
| - | 1DLJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_pyogenes Streptococcus pyogenes] with SO4, NAI, UGA and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http:// | + | 1DLJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_pyogenes Streptococcus pyogenes] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=NAI:'>NAI</scene>, <scene name='pdbligand=UGA:'>UGA</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DLJ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Streptococcus pyogenes]] | [[Category: Streptococcus pyogenes]] | ||
[[Category: UDP-glucose 6-dehydrogenase]] | [[Category: UDP-glucose 6-dehydrogenase]] | ||
| - | [[Category: Campbell, R | + | [[Category: Campbell, R E.]] |
| - | [[Category: Mosimann, S | + | [[Category: Mosimann, S C.]] |
| - | [[Category: Rijn, I | + | [[Category: Rijn, I van de.]] |
| - | [[Category: Strynadka, N | + | [[Category: Strynadka, N C.J.]] |
| - | [[Category: Tanner, M | + | [[Category: Tanner, M E.]] |
[[Category: GOL]] | [[Category: GOL]] | ||
[[Category: NAI]] | [[Category: NAI]] | ||
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[[Category: ternary complex]] | [[Category: ternary complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:17:51 2008'' |
Revision as of 10:17, 21 February 2008
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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 with , , and as ligands. Active as UDP-glucose 6-dehydrogenase, with EC number 1.1.1.22 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 Feb 21 12:17:51 2008
