1yfe: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
 
(11 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1yfe.gif|left|200px]]
<!--
The line below this paragraph, containing "STRUCTURE_1yfe", creates the "Structure Box" on the page.
You may change the PDB parameter (which sets the PDB file loaded into the applet)
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
or leave the SCENE parameter empty for the default display.
-->
{{STRUCTURE_1yfe|  PDB=1yfe  |  SCENE=  }}
'''Crystal structure of apo fumarase C from Escherichia coli'''


==Crystal structure of apo fumarase C from Escherichia coli==
<StructureSection load='1yfe' size='340' side='right'caption='[[1yfe]], [[Resolution|resolution]] 2.19&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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 ==
[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]]
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.


==Overview==
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>
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==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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].
</div>
<div class="pdbe-citations 1yfe" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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]
*[[Fumarase|Fumarase]]
[[Category: Escherichia coli]]
== References ==
[[Category: Fumarate hydratase]]
<references/>
[[Category: Single protein]]
__TOC__
[[Category: Weaver, T.]]
</StructureSection>
[[Category: Allosteric]]
[[Category: Escherichia coli K-12]]
[[Category: Apo]]
[[Category: Large Structures]]
[[Category: Fumarase]]
[[Category: Weaver T]]
[[Category: Kreb's cycle]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 16:15:17 2008''