1nzc
From Proteopedia
(New page: 200px<br /><applet load="1nzc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nzc, resolution 1.80Å" /> '''The high resolution ...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1nzc.jpg|left|200px]]<br /><applet load="1nzc" size=" | + | [[Image:1nzc.jpg|left|200px]]<br /><applet load="1nzc" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1nzc, resolution 1.80Å" /> | caption="1nzc, resolution 1.80Å" /> | ||
'''The high resolution structures of RmlC from Streptococcus suis in complex with dTDP-D-xylose'''<br /> | '''The high resolution structures of RmlC from Streptococcus suis in complex with dTDP-D-xylose'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Nature achieves the epimerization of carbohydrates by a variety of | + | Nature achieves the epimerization of carbohydrates by a variety of chemical routes. One common route is that performed by the class of enzyme defined by dTDP-6-deoxy-D-xylo-4-hexulose 3,5-epimerase (RmlC) from the rhamnose pathway. Earlier studies failed to identify the key residues in catalysis. We report the 1.3 A structure of RmlC from Streptococcus suis type 2 and its complexes with dTDP-D-glucose and dTDP-D-xylose. The streptococcal RmlC enzymes belong to a separate subgroup, sharing only 25% identity with RmlC from other bacteria, yet the S. suis enzyme has similar kinetic properties and structure to other RmlC enzymes. Structure, sequence alignment, and mutational analysis have now allowed reliable identification of the catalytic residues and their roles. |
==About this Structure== | ==About this Structure== | ||
| - | 1NZC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_suis Streptococcus suis] with NI and TDX as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/dTDP-4-dehydrorhamnose_3,5-epimerase dTDP-4-dehydrorhamnose 3,5-epimerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.1.3.13 5.1.3.13] Full crystallographic information is available from [http:// | + | 1NZC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_suis Streptococcus suis] with <scene name='pdbligand=NI:'>NI</scene> and <scene name='pdbligand=TDX:'>TDX</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/dTDP-4-dehydrorhamnose_3,5-epimerase dTDP-4-dehydrorhamnose 3,5-epimerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.1.3.13 5.1.3.13] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NZC OCA]. |
==Reference== | ==Reference== | ||
| Line 17: | Line 17: | ||
[[Category: Blankenfeldt, W.]] | [[Category: Blankenfeldt, W.]] | ||
[[Category: Dong, C.]] | [[Category: Dong, C.]] | ||
| - | [[Category: Major, L | + | [[Category: Major, L L.]] |
[[Category: Maskell, D.]] | [[Category: Maskell, D.]] | ||
| - | [[Category: Naismith, J | + | [[Category: Naismith, J H.]] |
[[Category: NI]] | [[Category: NI]] | ||
[[Category: TDX]] | [[Category: TDX]] | ||
[[Category: jelly roll-like structure; beta sheet]] | [[Category: jelly roll-like structure; beta sheet]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:11:42 2008'' |
Revision as of 12:11, 21 February 2008
|
The high resolution structures of RmlC from Streptococcus suis in complex with dTDP-D-xylose
Overview
Nature achieves the epimerization of carbohydrates by a variety of chemical routes. One common route is that performed by the class of enzyme defined by dTDP-6-deoxy-D-xylo-4-hexulose 3,5-epimerase (RmlC) from the rhamnose pathway. Earlier studies failed to identify the key residues in catalysis. We report the 1.3 A structure of RmlC from Streptococcus suis type 2 and its complexes with dTDP-D-glucose and dTDP-D-xylose. The streptococcal RmlC enzymes belong to a separate subgroup, sharing only 25% identity with RmlC from other bacteria, yet the S. suis enzyme has similar kinetic properties and structure to other RmlC enzymes. Structure, sequence alignment, and mutational analysis have now allowed reliable identification of the catalytic residues and their roles.
About this Structure
1NZC is a Single protein structure of sequence from Streptococcus suis with and as ligands. Active as dTDP-4-dehydrorhamnose 3,5-epimerase, with EC number 5.1.3.13 Full crystallographic information is available from OCA.
Reference
High-resolution structures of RmlC from Streptococcus suis in complex with substrate analogs locate the active site of this class of enzyme., Dong C, Major LL, Allen A, Blankenfeldt W, Maskell D, Naismith JH, Structure. 2003 Jun;11(6):715-23. PMID:12791259
Page seeded by OCA on Thu Feb 21 14:11:42 2008
