Proteopedia

1c8u: Difference between revisions

← Older edit
No edit summary
No edit summary
 
Line 3: Line 3:
<StructureSection load='1c8u' size='340' side='right'caption='[[1c8u]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='1c8u' size='340' side='right'caption='[[1c8u]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1c8u]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C8U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C8U FirstGlance]. <br>
<table><tr><td colspan='2'>[[1c8u]] 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=1C8U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C8U FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</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=1c8u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c8u OCA], [https://pdbe.org/1c8u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c8u RCSB], [https://www.ebi.ac.uk/pdbsum/1c8u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c8u ProSAT]</span></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=1c8u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c8u OCA], [https://pdbe.org/1c8u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c8u RCSB], [https://www.ebi.ac.uk/pdbsum/1c8u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c8u ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/TESB_ECOLI TESB_ECOLI]] Can hydrolyze a broad range of acyl-CoA thioesters. Its physiological function is not known.  
[https://www.uniprot.org/uniprot/TESB_ECOLI TESB_ECOLI] Can hydrolyze a broad range of acyl-CoA thioesters. Its physiological function is not known.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 19: Line 20:
</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=1c8u ConSurf].
</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=1c8u ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Here we report the solution and refinement at 1.9 A resolution of the crystal structure of the Escherichia coli medium chain length acyl-CoA thioesterase II. This enzyme is a close homolog of the human protein that interacts with the product of the HIV-1 Nef gene, sharing 45% amino acid sequence identity with it. The structure of the E. coli thioesterase II reveals a new tertiary fold, a 'double hot dog', showing an internal repeat with a basic unit that is structurally similar to the recently described beta-hydroxydecanoyl thiol ester dehydrase. The catalytic site, inferred from the crystal structure and verified by site directed mutagenesis, involves novel chemistry and includes Asp 204, Gln 278 and Thr 228, which synergistically activate a nucleophilic water molecule.
Crystal structure of the Escherichia coli thioesterase II, a homolog of the human Nef binding enzyme.,Li J, Derewenda U, Dauter Z, Smith S, Derewenda ZS Nat Struct Biol. 2000 Jul;7(7):555-9. PMID:10876240<ref>PMID:10876240</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1c8u" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Thioesterase 3D structures|Thioesterase 3D structures]]
*[[Thioesterase 3D structures|Thioesterase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus coli migula 1895]]
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Derewenda, Z S]]
[[Category: Derewenda ZS]]
[[Category: Li, J]]
[[Category: Li J]]
[[Category: Hydrolase]]
[[Category: Internal repeat]]

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/w/1c8u"