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[[Image:1yfe.gif|left|200px]]


{{Structure
==Crystal structure of apo fumarase C from Escherichia coli==
|PDB= 1yfe |SIZE=350|CAPTION= <scene name='initialview01'>1yfe</scene>, resolution 2.19&Aring;
<StructureSection load='1yfe' size='340' side='right'caption='[[1yfe]], [[Resolution|resolution]] 2.19&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<table><tr><td colspan='2'>[[1yfe]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YFE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YFE FirstGlance]. <br>
|ACTIVITY= [http://en.wikipedia.org/wiki/Fumarate_hydratase Fumarate hydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.2 4.2.1.2]  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.19&#8491;</td></tr>
|GENE=  
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1yfe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yfe OCA], [https://pdbe.org/1yfe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yfe RCSB], [https://www.ebi.ac.uk/pdbsum/1yfe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yfe ProSAT]</span></td></tr>
}}
</table>
 
== Function ==
'''Crystal structure of apo fumarase C from Escherichia coli'''
[https://www.uniprot.org/uniprot/FUMC_ECOLI FUMC_ECOLI] Catalyzes the reversible addition of water to fumarate to give L-malate.<ref>PMID:1917897</ref>
 
== Evolutionary Conservation ==
 
[[Image:Consurf_key_small.gif|200px|right]]
==Overview==
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/yf/1yfe_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=1yfe ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Previous crystal structures of fumarase C from Escherichia coli have noted two occupied dicarboxylate-binding sites termed the active site and the B site. Here, the first known fumarase C structure is reported in which both sites are unoccupied by bound ligand. This so-called ;free' crystal form shows conservation of the active-site water in a similar orientation to that reported in other fumarase C crystal structures. More importantly, a shift of His129 has been observed at the B site. This new crystallographic information suggests the use of water as a permanent member of the active site and the use of an imidazole-imidazolium conversion to control access at the allosteric B site.
Previous crystal structures of fumarase C from Escherichia coli have noted two occupied dicarboxylate-binding sites termed the active site and the B site. Here, the first known fumarase C structure is reported in which both sites are unoccupied by bound ligand. This so-called ;free' crystal form shows conservation of the active-site water in a similar orientation to that reported in other fumarase C crystal structures. More importantly, a shift of His129 has been observed at the B site. This new crystallographic information suggests the use of water as a permanent member of the active site and the use of an imidazole-imidazolium conversion to control access at the allosteric B site.


==About this Structure==
Structure of free fumarase C from Escherichia coli.,Weaver T Acta Crystallogr D Biol Crystallogr. 2005 Oct;61(Pt 10):1395-401. Epub, 2005 Sep 28. PMID:16204892<ref>PMID:16204892</ref>
1YFE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YFE OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Structure of free fumarase C from Escherichia coli., Weaver T, Acta Crystallogr D Biol Crystallogr. 2005 Oct;61(Pt 10):1395-401. Epub, 2005 Sep 28. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16204892 16204892]
</div>
[[Category: Escherichia coli]]
<div class="pdbe-citations 1yfe" style="background-color:#fffaf0;"></div>
[[Category: Fumarate hydratase]]
[[Category: Single protein]]
[[Category: Weaver, T.]]
[[Category: allosteric]]
[[Category: apo]]
[[Category: fumarase]]
[[Category: kreb's cycle]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:22:09 2008''
==See Also==
*[[Fumarase|Fumarase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Weaver T]]

Latest revision as of 06:56, 23 August 2023

Crystal structure of apo fumarase C from Escherichia coli

1yfe, resolution 2.19Å

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