3ao0: Difference between revisions

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[[Image:3ao0.jpg|left|200px]]


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==Crystal structure of ethanolamine ammonia-lyase from Escherichia coli complexed with CN-CBL and (S)-2-amino-1-propanol==
The line below this paragraph, containing "STRUCTURE_3ao0", creates the "Structure Box" on the page.
<StructureSection load='3ao0' size='340' side='right'caption='[[3ao0]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[3ao0]] is a 4 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=3AO0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AO0 FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25&#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=2A1:(2S)-2-AMINOPROPAN-1-OL'>2A1</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
{{STRUCTURE_3ao0|  PDB=3ao0  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ao0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ao0 OCA], [https://pdbe.org/3ao0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ao0 RCSB], [https://www.ebi.ac.uk/pdbsum/3ao0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ao0 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/EUTB_ECOLI EUTB_ECOLI]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Coenzyme B(12)-dependent ethanolamine ammonia-lyase acts on both enantiomers of the substrate 2-amino-1-propanol [Diziol, P., et al. (1980) Eur. J. Biochem. 106, 211-224]. To rationalize this apparent lack of stereospecificity and the enantiomer-specific stereochemical courses of the deamination, we analyzed the X-ray structures of enantiomer-bound forms of the enzyme-cyanocobalamin complex. The lower affinity for the (R)-enantiomer may be due to the conformational change of the Valalpha326 side chain of the enzyme. In a manner consistent with the reported experimental results, we can predict that the pro-S hydrogen atom on C1 is abstracted by the adenosyl radical from both enantiomeric substrates, because it is the nearest one in both enantiomer-bound forms. We also predicted that the NH(2) group migrates from C2 to C1 by a suprafacial shift, with inversion of configuration at C1 for both enantiomeric substrates, although the absolute configuration of the 1-amino-1-propanol intermediate is not yet known. Reported labeling experiments demonstrate that (R)-2-amino-1-propanol is deaminated by the enzyme with inversion of configuration at C2, whereas the (S)-enantiomer is deaminated with retention. By taking these results into consideration, we can predict the rotameric radical intermediate from the (S)-enantiomer undergoes flipping to the rotamer from the (R)-enantiomer before the hydrogen back-abstraction. This suggests the preference of the enzyme active site for the rotamer from the (R)-enantiomer in equilibration. This preference might be explained in terms of the steric repulsion of the (S)-enantiomer-derived product radical at C3 with the Phealpha329 and Leualpha402 residues.


===Crystal structure of ethanolamine ammonia-lyase from Escherichia coli complexed with CN-CBL and (S)-2-amino-1-propanol===
How coenzyme B12-dependent ethanolamine ammonia-lyase deals with both enantiomers of 2-amino-1-propanol as substrates: structure-based rationalization.,Shibata N, Higuchi Y, Toraya T Biochemistry. 2011 Feb 1;50(4):591-8. Epub 2010 Dec 30. PMID:21142024<ref>PMID:21142024</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The line below this paragraph, {{ABSTRACT_PUBMED_21142024}}, adds the Publication Abstract to the page
<div class="pdbe-citations 3ao0" style="background-color:#fffaf0;"></div>
(as it appears on PubMed at http://www.pubmed.gov), where 21142024 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_21142024}}
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</StructureSection>
==About this Structure==
[[Category: Escherichia coli K-12]]
[[3ao0]] is a 4 chain structure with 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=3AO0 OCA].
[[Category: Large Structures]]
 
[[Category: Shibata N]]
==Reference==
<ref group="xtra">PMID:021142024</ref><references group="xtra"/>
[[Category: Escherichia coli]]
[[Category: Ethanolamine ammonia-lyase]]
[[Category: Shibata, N.]]
[[Category: Cobalamin]]
[[Category: Cobalt]]
[[Category: Lyase]]
[[Category: Tim barrel]]
Retrieved from "https://proteopedia.org/3ao0"