1dli: Difference between revisions

Line 1:

[[Image:1dli.gif|left|200px]]<br /><applet load="1dli" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1dli.gif|left|200px]]<br /><applet load="1dli" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1dli, resolution 2.31Å" />

'''THE FIRST STRUCTURE OF UDP-GLUCOSE DEHYDROGENASE (UDPGDH) REVEALS THE CATALYTIC RESIDUES NECESSARY FOR THE TWO-FOLD OXIDATION'''<br />

==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.

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 [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_pyogenes Streptococcus pyogenes] with SO4, NAD, UDX 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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1DLI OCA].

1DLI 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=NAD:'>NAD</scene>, <scene name='pdbligand=UDX:'>UDX</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=1DLI OCA].

==Reference==

Line 14:

[[Category: Streptococcus pyogenes]]

[[Category: UDP-glucose 6-dehydrogenase]]

[[Category: Campbell, R.E.]]

[[Category: Campbell, R E.]]

[[Category: Mosimann, S.C.]]

[[Category: Mosimann, S C.]]

[[Category: Rijn, I.van.de.]]

[[Category: Rijn, I van de.]]

[[Category: Strynadka, N.C.J.]]

[[Category: Strynadka, N C.J.]]

[[Category: Tanner, M.E.]]

[[Category: Tanner, M E.]]

[[Category: GOL]]

[[Category: NAD]]

Line 27:

[[Category: ternary complex]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:17:51 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1dli.gif|left|200px]]<br /><applet load="1dli" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1dli.gif|left|200px]]<br /><applet load="1dli" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1dli, resolution 2.31&Aring;" />
 '''THE FIRST STRUCTURE OF UDP-GLUCOSE DEHYDROGENASE (UDPGDH) REVEALS THE CATALYTIC RESIDUES NECESSARY FOR THE TWO-FOLD OXIDATION'''<br />
 ==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.
+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==
-DLI 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, NAD, UDX 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DLI OCA].
+DLI 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=NAD:'>NAD</scene>, <scene name='pdbligand=UDX:'>UDX</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=1DLI OCA].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: Streptococcus pyogenes]]
 [[Category: UDP-glucose 6-dehydrogenase]]
-[[Category: Campbell, R.E.]]
+[[Category: Campbell, R E.]]
-[[Category: Mosimann, S.C.]]
+[[Category: Mosimann, S C.]]
-[[Category: Rijn, I.van.de.]]
+[[Category: Rijn, I van de.]]
-[[Category: Strynadka, N.C.J.]]
+[[Category: Strynadka, N C.J.]]
-[[Category: Tanner, M.E.]]
+[[Category: Tanner, M E.]]
 [[Category: GOL]]
 [[Category: NAD]]
@@ Line 27: / Line 27: @@
 [[Category: ternary complex]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:23:11 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:17:51 2008''