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==NEUROSPORA CRASSA CATALASE-3 EXPRESSED IN E. COLI, ORTHORHOMBIC FORM.==
==NEUROSPORA CRASSA CATALASE-3 EXPRESSED IN E. COLI, ORTHORHOMBIC FORM.==
<StructureSection load='3zj5' size='340' side='right' caption='[[3zj5]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
<StructureSection load='3zj5' size='340' side='right'caption='[[3zj5]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3zj5]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Chrysonilia_crassa Chrysonilia crassa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZJ5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ZJ5 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3zj5]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Chrysonilia_crassa Chrysonilia crassa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZJ5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZJ5 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AE3:2-(2-ETHOXYETHOXY)ETHANOL'>AE3</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=TAR:D(-)-TARTARIC+ACID'>TAR</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AE3:2-(2-ETHOXYETHOXY)ETHANOL'>AE3</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=TAR:D(-)-TARTARIC+ACID'>TAR</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3zj4|3zj4]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3zj4|3zj4]]</div></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Catalase Catalase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.6 1.11.1.6] </span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Catalase Catalase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.6 1.11.1.6] </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=3zj5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zj5 OCA], [http://pdbe.org/3zj5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3zj5 RCSB], [http://www.ebi.ac.uk/pdbsum/3zj5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3zj5 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=3zj5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zj5 OCA], [https://pdbe.org/3zj5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zj5 RCSB], [https://www.ebi.ac.uk/pdbsum/3zj5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zj5 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/CAT3_NEUCR CAT3_NEUCR]] Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide (By similarity).  
[[https://www.uniprot.org/uniprot/CAT3_NEUCR CAT3_NEUCR]] Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide (By similarity).  
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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==See Also==
==See Also==
*[[Catalase|Catalase]]
*[[Catalase 3D structures|Catalase 3D structures]]
== References ==
== References ==
<references/>
<references/>
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[[Category: Catalase]]
[[Category: Catalase]]
[[Category: Chrysonilia crassa]]
[[Category: Chrysonilia crassa]]
[[Category: Large Structures]]
[[Category: Rudino-Pinera, E]]
[[Category: Rudino-Pinera, E]]
[[Category: Zarate-Romero, A]]
[[Category: Zarate-Romero, A]]

Revision as of 08:48, 10 August 2022

NEUROSPORA CRASSA CATALASE-3 EXPRESSED IN E. COLI, ORTHORHOMBIC FORM.NEUROSPORA CRASSA CATALASE-3 EXPRESSED IN E. COLI, ORTHORHOMBIC FORM.

Structural highlights

3zj5 is a 4 chain structure with sequence from Chrysonilia crassa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, , , ,
Activity:Catalase, with EC number 1.11.1.6
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CAT3_NEUCR] Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide (By similarity).

Publication Abstract from PubMed

Polymorphism is frequently observed from different crystallization conditions. In proteins, the effect on conformational variability is poorly documented, with only a few reported examples. Here, three polymorphic crystal structures determined for a large-subunit catalase, CAT-3 from Neurospora crassa, are reported. Two of them belonged to new space groups, P1 and P43212, and a third structure belonged to the same space group, P212121, as the previously deposited 2.3 A resolution structure (PDB entry 3ej6), but had a higher resolution (1.95 A). Comparisons between these polymorphic structures highlight the conformational stability of tetrameric CAT-3 and reveal a distortion in the tetrameric structure that has not previously been described.

Conformational stability and crystal packing: polymorphism in Neurospora crassa CAT-3.,Zarate-Romero A, Stojanoff V, Rojas-Trejo SP, Hansberg W, Rudino-Pinera E Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Jul 1;69(Pt 7):753-8. doi:, 10.1107/S1744309113013468. Epub 2013 Jun 27. PMID:23832201[1]

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

See Also

References

  1. Zarate-Romero A, Stojanoff V, Rojas-Trejo SP, Hansberg W, Rudino-Pinera E. Conformational stability and crystal packing: polymorphism in Neurospora crassa CAT-3. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Jul 1;69(Pt 7):753-8. doi:, 10.1107/S1744309113013468. Epub 2013 Jun 27. PMID:23832201 doi:10.1107/S1744309113013468

3zj5, resolution 1.95Å

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