This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

1hnu

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 10:51, 4 August 2021

CRYSTAL STRUCTURE OF PEROXISOMAL DELTA3-DELTA2-ENOYL-COA ISOMERASE FROM SACCHAROMYCES CEREVISIAE

Structural highlights

1hnu is a 1 chain structure with sequence from Atcc 18824. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	1hno
Activity:	Dodecenoyl-CoA isomerase, with EC number 5.3.3.8
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ECI1_YEAST] Essential for the beta oxidation of unsaturated fatty acids.^[1]

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

The active-site geometry of the first crystal structure of a Delta(3)-Delta(2)-enoyl-coenzyme A (CoA) isomerase (the peroxisomal enzyme from the yeast Saccharomyces cerevisiae) shows that only one catalytic base, Glu158, is involved in shuttling the proton from the C2 carbon atom of the substrate, Delta(3)-enoyl-CoA, to the C4 atom of the product, Delta(2)-enoyl-CoA. Site-directed mutagenesis has been performed to confirm that this glutamate residue is essential for catalysis. This Delta(3)-Delta(2)-enoyl-CoA isomerase is a hexameric enzyme, consisting of six identical subunits. It belongs to the hydratase/isomerase superfamily of enzymes which catalyze a wide range of CoA-dependent reactions. The members of the hydratase/ isomerase superfamily have only a low level of sequence identity. Comparison of the crystal structure of the Delta(3)-Delta(2)-enoyl-CoA isomerase with the other structures of this superfamily shows only one region of large structural variability, which is in the second turn of the spiral fold and which is involved in defining the shape of the binding pocket.

The crystal structure of delta(3)-delta(2)-enoyl-CoA isomerase.,Mursula AM, van Aalten DM, Hiltunen JK, Wierenga RK J Mol Biol. 2001 Jun 15;309(4):845-53. PMID:11399063^[2]

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

References

↑ Geisbrecht BV, Zhu D, Schulz K, Nau K, Morrell JC, Geraghty M, Schulz H, Erdmann R, Gould SJ. Molecular characterization of Saccharomyces cerevisiae Delta3, Delta2-enoyl-CoA isomerase. J Biol Chem. 1998 Dec 11;273(50):33184-91. PMID:9837886
↑ Mursula AM, van Aalten DM, Hiltunen JK, Wierenga RK. The crystal structure of delta(3)-delta(2)-enoyl-CoA isomerase. J Mol Biol. 2001 Jun 15;309(4):845-53. PMID:11399063 doi:10.1006/jmbi.2001.4671

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 3: / Line 3: @@
 <StructureSection load='1hnu' size='340' side='right'caption='[[1hnu]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1hnu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HNU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HNU FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1hnu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HNU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HNU FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=REO:PERRHENATE'>REO</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=REO:PERRHENATE'>REO</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1hno|1hno]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1hno|1hno]]</div></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dodecenoyl-CoA_isomerase Dodecenoyl-CoA isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.3.8 5.3.3.8] </span></td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Dodecenoyl-CoA_isomerase Dodecenoyl-CoA isomerase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.3.8 5.3.3.8] </span></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=1hnu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hnu OCA], [http://pdbe.org/1hnu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hnu RCSB], [http://www.ebi.ac.uk/pdbsum/1hnu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1hnu 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=1hnu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hnu OCA], [https://pdbe.org/1hnu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hnu RCSB], [https://www.ebi.ac.uk/pdbsum/1hnu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hnu ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/ECI1_YEAST ECI1_YEAST]] Essential for the beta oxidation of unsaturated fatty acids.<ref>PMID:9837886</ref>
+[[https://www.uniprot.org/uniprot/ECI1_YEAST ECI1_YEAST]] Essential for the beta oxidation of unsaturated fatty acids.<ref>PMID:9837886</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1hnu

From Proteopedia

Revision as of 10:51, 4 August 2021

CRYSTAL STRUCTURE OF PEROXISOMAL DELTA3-DELTA2-ENOYL-COA ISOMERASE FROM SACCHAROMYCES CEREVISIAE

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox