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1h6j
From Proteopedia
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| - | [[Image:1h6j.gif|left|200px]] | ||
| - | + | ==The three-dimensional structure of capsule-specific CMP:2-keto-3-deoxy-manno-octonic acid synthetase from Escherichia coli== | |
| - | + | <StructureSection load='1h6j' size='340' side='right'caption='[[1h6j]], [[Resolution|resolution]] 2.32Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[1h6j]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H6J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H6J FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.32Å</td></tr> | |
| - | | | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1h6j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h6j OCA], [https://pdbe.org/1h6j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h6j RCSB], [https://www.ebi.ac.uk/pdbsum/1h6j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h6j ProSAT]</span></td></tr> |
| - | + | </table> | |
| - | + | == Function == | |
| - | + | [https://www.uniprot.org/uniprot/KPSU5_ECOLX KPSU5_ECOLX] Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria. | |
| - | + | == Evolutionary Conservation == | |
| - | + | [[Image:Consurf_key_small.gif|200px|right]] | |
| - | == | + | Check<jmol> |
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h6/1h6j_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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=1h6j ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
CMP-Kdo synthetases from Gram-negative bacteria activate Kdo for incorporation into lipo- and capsule-polysaccharides. Here we report the crystal structure of the capsule-specific synthetase from E. coli at 2.3 A resolution. The enzyme is a dimer of 2 x 245 amino acid residues assuming C2 symmetry. It contains a central predominantly parallel beta-sheet with surrounding helices. The chain fold is novel; it is remotely related to a double Rossmann fold. A large pocket at the carboxyl terminal ends of the central. beta-strands most likely accommodates the catalytic center. A putative phosphate binding site at the loop between the first beta-strand and the following helix is indicated by a bound iridium hexachloride anion. | CMP-Kdo synthetases from Gram-negative bacteria activate Kdo for incorporation into lipo- and capsule-polysaccharides. Here we report the crystal structure of the capsule-specific synthetase from E. coli at 2.3 A resolution. The enzyme is a dimer of 2 x 245 amino acid residues assuming C2 symmetry. It contains a central predominantly parallel beta-sheet with surrounding helices. The chain fold is novel; it is remotely related to a double Rossmann fold. A large pocket at the carboxyl terminal ends of the central. beta-strands most likely accommodates the catalytic center. A putative phosphate binding site at the loop between the first beta-strand and the following helix is indicated by a bound iridium hexachloride anion. | ||
| - | + | The three-dimensional structure of capsule-specific CMP: 2-keto-3-deoxy-manno-octonic acid synthetase from Escherichia coli.,Jelakovic S, Jann K, Schulz GE FEBS Lett. 1996 Aug 5;391(1-2):157-61. PMID:8706906<ref>PMID:8706906</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1h6j" style="background-color:#fffaf0;"></div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Jann | + | [[Category: Jann K]] |
| - | [[Category: Jelakovic | + | [[Category: Jelakovic S]] |
| - | [[Category: Schulz | + | [[Category: Schulz GE]] |
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Current revision
The three-dimensional structure of capsule-specific CMP:2-keto-3-deoxy-manno-octonic acid synthetase from Escherichia coli
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