1ey3: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
New page: left|200px<br /><applet load="1ey3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ey3, resolution 2.3Å" /> '''STRUCTURE OF ENOYL-CO...
 
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
 
(17 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1ey3.gif|left|200px]]<br /><applet load="1ey3" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1ey3, resolution 2.3&Aring;" />
'''STRUCTURE OF ENOYL-COA HYDRATASE COMPLEXED WITH THE SUBSTRATE DAC-COA'''<br />


==Overview==
==STRUCTURE OF ENOYL-COA HYDRATASE COMPLEXED WITH THE SUBSTRATE DAC-COA==
We have determined the crystal structure of the enzyme enoyl-CoA hydratase, (ECH) from rat liver with the bound substrate, 4-(N,N-dimethylamino)cinnamoyl-CoA using X-ray diffraction data to a, resolution of 2.3 A. In addition to the thiolester substrate, the, catalytic water, which is added in the hydration reaction, has been, modeled into well-defined electron density in each of the six active sites, of the physiological hexamer within the crystallographic asymmetric unit., The catalytic water bridges Glu(144) and Glu(164) of the enzyme and has a, lone pair of electrons poised to react with C(3) of the enzyme-bound, alpha,beta-unsaturated thiolester. The water molecule, which bridges two, glutamate residues, is reminiscent of the enolase active site. However, unlike enolase, which has a lysine available to donate a proton, there are, no other sources of protons available from other active site residues in, ECH. Furthermore, an analysis of the hydrogen-bonding network of the, active site suggests that both Glu(144) and Glu(164) are ionized and carry, a negative charge with no reasonable place to have a protonated, carboxylate. This lack of hydrogen-bonding acceptors that could, accommodate a source of a proton, other than from the water molecule, leads to a hypothesis that the three atoms from a single water molecule, are added across the double bond to form the hydrated product. The, structural results are discussed in connection with details of the, mechanism, which have been elucidated from kinetics, site-directed, mutagenesis, and spectroscopy of enzyme-substrate species, in presenting, an atomic-resolution mechanism of the reaction. Contrary to the previous, interpretation, the structure of the E-S complex together with previously, determined kinetic isotope effects is consistent with either a concerted, mechanism or an E1cb stepwise mechanism.
<StructureSection load='1ey3' size='340' side='right'caption='[[1ey3]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ey3]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EY3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EY3 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]] 2.3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DAK:4-(N,N-DIMETHYLAMINO)CINNAMOYL-COA'>DAK</scene></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=1ey3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ey3 OCA], [https://pdbe.org/1ey3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ey3 RCSB], [https://www.ebi.ac.uk/pdbsum/1ey3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ey3 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ECHM_RAT ECHM_RAT] Straight-chain enoyl-CoA thioesters from C4 up to at least C16 are processed, although with decreasing catalytic rate.
== 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/ey/1ey3_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=1ey3 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1EY3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with DAK as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Enoyl-CoA_hydratase Enoyl-CoA hydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.17 4.2.1.17] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EY3 OCA].
*[[Enoyl-CoA hydratase 3D structures|Enoyl-CoA hydratase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Structural mechanism of enoyl-CoA hydratase: three atoms from a single water are added in either an E1cb stepwise or concerted fashion., Bahnson BJ, Anderson VE, Petsko GA, Biochemistry. 2002 Feb 26;41(8):2621-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11851409 11851409]
[[Category: Large Structures]]
[[Category: Enoyl-CoA hydratase]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Anderson VE]]
[[Category: Anderson, V.E.]]
[[Category: Bahnson BJ]]
[[Category: Bahnson, B.J.]]
[[Category: Petsko GA]]
[[Category: Petsko, G.A.]]
[[Category: DAK]]
[[Category: beta-elimination]]
[[Category: beta-oxidation]]
[[Category: concerted reaction]]
[[Category: crotonase]]
[[Category: enoyl-coa hydratase]]
[[Category: fatty acid metabolism]]
[[Category: syn-addition]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:25:00 2007''

Latest revision as of 13:22, 13 March 2024

STRUCTURE OF ENOYL-COA HYDRATASE COMPLEXED WITH THE SUBSTRATE DAC-COA

1ey3, resolution 2.30Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1ey3&oldid=4087209"