1nzc

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(New page: 200px<br /><applet load="1nzc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nzc, resolution 1.80&Aring;" /> '''The high resolution ...)
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[[Image:1nzc.jpg|left|200px]]<br /><applet load="1nzc" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1nzc, resolution 1.80&Aring;" />
 
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'''The high resolution structures of RmlC from Streptococcus suis in complex with dTDP-D-xylose'''<br />
 
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==Overview==
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==The high resolution structures of RmlC from Streptococcus suis in complex with dTDP-D-xylose==
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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.
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<StructureSection load='1nzc' size='340' side='right'caption='[[1nzc]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1nzc]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_suis Streptococcus suis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NZC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NZC FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=TDX:THYMIDINE-5-DIPHOSPHO-BETA-D-XYLOSE'>TDX</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1nzc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nzc OCA], [https://pdbe.org/1nzc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nzc RCSB], [https://www.ebi.ac.uk/pdbsum/1nzc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nzc ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q8GIQ0_STRSU Q8GIQ0_STRSU]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nz/1nzc_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1nzc ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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>
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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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NZC OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12791259 12791259]
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</div>
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[[Category: Single protein]]
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<div class="pdbe-citations 1nzc" style="background-color:#fffaf0;"></div>
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[[Category: Streptococcus suis]]
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[[Category: dTDP-4-dehydrorhamnose 3,5-epimerase]]
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[[Category: Allen, A.]]
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[[Category: Blankenfeldt, W.]]
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[[Category: Dong, C.]]
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[[Category: Major, L.L.]]
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[[Category: Maskell, D.]]
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[[Category: Naismith, J.H.]]
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[[Category: NI]]
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[[Category: TDX]]
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[[Category: jelly roll-like structure; beta sheet]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 00:06:03 2007''
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==See Also==
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*[[RmlC|RmlC]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Streptococcus suis]]
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[[Category: Allen A]]
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[[Category: Blankenfeldt W]]
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[[Category: Dong C]]
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[[Category: Major LL]]
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[[Category: Maskell D]]
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[[Category: Naismith JH]]

Current revision

The high resolution structures of RmlC from Streptococcus suis in complex with dTDP-D-xylose

PDB ID 1nzc

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