1nxm
From Proteopedia
(New page: 200px<br /><applet load="1nxm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nxm, resolution 1.30Å" /> '''The high resolution ...) |
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| - | [[Image:1nxm.gif|left|200px]]<br /><applet load="1nxm" size=" | + | [[Image:1nxm.gif|left|200px]]<br /><applet load="1nxm" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1nxm, resolution 1.30Å" /> | caption="1nxm, resolution 1.30Å" /> | ||
'''The high resolution structures of RmlC from Streptococcus suis'''<br /> | '''The high resolution structures of RmlC from Streptococcus suis'''<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== | ||
| - | 1NXM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_suis Streptococcus suis]. 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:// | + | 1NXM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_suis Streptococcus suis]. 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=1NXM OCA]. |
==Reference== | ==Reference== | ||
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[[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: 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 14:11:08 2008'' |
Revision as of 12:11, 21 February 2008
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The high resolution structures of RmlC from Streptococcus suis
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
1NXM is a Single protein structure of sequence from Streptococcus suis. 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
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