1c8u

From Proteopedia

(Difference between revisions)

Revision as of 10:34, 14 July 2021

CRYSTAL STRUCTURE OF THE E.COLI THIOESTERASE II, A HOMOLOGUE OF THE HUMAN NEF-BINDING ENZYME

Structural highlights

1c8u is a 2 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[TESB_ECOLI] Can hydrolyze a broad range of acyl-CoA thioesters. Its physiological function is not known.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Li J, Derewenda U, Dauter Z, Smith S, Derewenda ZS. Crystal structure of the Escherichia coli thioesterase II, a homolog of the human Nef binding enzyme. Nat Struct Biol. 2000 Jul;7(7):555-9. PMID:10876240 doi:10.1038/76776

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1c8u"

@@ Line 3: / Line 3: @@
 <StructureSection load='1c8u' size='340' side='right'caption='[[1c8u]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1c8u]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/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/"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>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene></td></tr>
+</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1c8u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c8u OCA], [http://pdbe.org/1c8u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1c8u RCSB], [http://www.ebi.ac.uk/pdbsum/1c8u PDBsum], [http://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>
 == Function ==
-[[http://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 ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 30: / Line 30: @@
 ==See Also==
-*[[Thioesterase|Thioesterase]]
+*[[Thioesterase 3D structures|Thioesterase 3D structures]]
 == References ==
 <references/>

1c8u

From Proteopedia

Revision as of 10:34, 14 July 2021

CRYSTAL STRUCTURE OF THE E.COLI THIOESTERASE II, A HOMOLOGUE OF THE HUMAN NEF-BINDING ENZYME

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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