1h6j: Difference between revisions

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New page: left|200px<br /><applet load="1h6j" size="450" color="white" frame="true" align="right" spinBox="true" caption="1h6j, resolution 2.32Å" /> '''THE THREE-DIMENSIONA...
 
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[[Image:1h6j.gif|left|200px]]<br /><applet load="1h6j" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1h6j, resolution 2.32&Aring;" />
'''THE THREE-DIMENSIONAL STRUCTURE OF CAPSULE-SPECIFIC CMP:2-KETO-3-DEOXY-MANNO-OCTONIC ACID SYNTHETASE FROM ESCHERICHIA COLI'''<br />


==Overview==
==The three-dimensional structure of capsule-specific CMP:2-keto-3-deoxy-manno-octonic acid synthetase from Escherichia coli==
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.
<StructureSection load='1h6j' size='340' side='right'caption='[[1h6j]], [[Resolution|resolution]] 2.32&Aring;' 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]] 2.32&#8491;</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.


==About this Structure==
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>
1H6J is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/3-deoxy-manno-octulosonate_cytidylyltransferase 3-deoxy-manno-octulosonate cytidylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.38 2.7.7.38] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H6J OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8706906 8706906]
</div>
[[Category: 3-deoxy-manno-octulosonate cytidylyltransferase]]
<div class="pdbe-citations 1h6j" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Jann, K.]]
[[Category: Jann K]]
[[Category: Jelakovic, S.]]
[[Category: Jelakovic S]]
[[Category: Schulz, G.E.]]
[[Category: Schulz GE]]
[[Category: capsular polysaccharide]]
[[Category: cmp-kdo synthetase]]
[[Category: saccharide activation]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:26:12 2007''

Latest revision as of 08:54, 9 May 2024

The three-dimensional structure of capsule-specific CMP:2-keto-3-deoxy-manno-octonic acid synthetase from Escherichia coli

1h6j, resolution 2.32Å

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