1nxm
From Proteopedia
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|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= | ||
| - | |ACTIVITY= [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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= rmlc ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1307 Streptococcus suis]) | |GENE= rmlc ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1307 Streptococcus suis]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1nyw|1NYW]], [[1nzc|1NZC]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nxm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nxm OCA], [http://www.ebi.ac.uk/pdbsum/1nxm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1nxm RCSB]</span> | ||
}} | }} | ||
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[[Category: Maskell, D.]] | [[Category: Maskell, D.]] | ||
[[Category: Naismith, J H.]] | [[Category: Naismith, J H.]] | ||
| - | [[Category: jelly roll-like structure | + | [[Category: beta sheet]] |
| + | [[Category: jelly roll-like structure]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:36:58 2008'' |
Revision as of 19:37, 30 March 2008
| |||||||
| , resolution 1.30Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | rmlc (Streptococcus suis) | ||||||
| Activity: | dTDP-4-dehydrorhamnose 3,5-epimerase, with EC number 5.1.3.13 | ||||||
| Related: | 1NYW, 1NZC
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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