1nxm

<table><tr><td colspan='2'>[[1nxm]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43765 Atcc 43765]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NXM OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1NXM FirstGlance]. <br>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1nyw|1nyw]], [[1nzc|1nzc]]</div></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rmlc ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1307 ATCC 43765])</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1nxm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nxm OCA], [http://pdbe.org/1nxm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1nxm RCSB], [http://www.ebi.ac.uk/pdbsum/1nxm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1nxm ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:12791259</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1nxm" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Atcc 43765]]

[[Category: DTDP-4-dehydrorhamnose 3,5-epimerase]]

[[Category: Allen, A]]

[[Category: Blankenfeldt, W]]

[[Category: Dong, C]]

[[Category: Major, L L]]

[[Category: Maskell, D]]

[[Category: Naismith, J H]]

[[Category: Jelly roll-like structure]]