7qy6: Difference between revisions

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'''Unreleased structure'''


The entry 7qy6 is ON HOLD  until Paper Publication
==Structure of E.coli Class 2 L-asparaginase EcAIII, wild type (WT EcAIII)==
 
<StructureSection load='7qy6' size='340' side='right'caption='[[7qy6]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
Authors: Loch, J.I., Klonecka, A., Kadziolka, K., Bonarek, P., Barciszewski, J., Imiolczyk, B., Brzezinski, K., Jaskolski, M.
== Structural highlights ==
 
<table><tr><td colspan='2'>[[7qy6]] is a 4 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=7QY6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QY6 FirstGlance]. <br>
Description: Structure of E.coli Class 2 L-asparaginase EcAIII, wild type (WT EcAIII)
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65&#8491;</td></tr>
[[Category: Unreleased Structures]]
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
[[Category: Loch, J.I]]
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7qy6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qy6 OCA], [https://pdbe.org/7qy6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qy6 RCSB], [https://www.ebi.ac.uk/pdbsum/7qy6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qy6 ProSAT]</span></td></tr>
[[Category: Brzezinski, K]]
</table>
[[Category: Barciszewski, J]]
== Function ==
[[Category: Klonecka, A]]
[https://www.uniprot.org/uniprot/IAAA_ECOLI IAAA_ECOLI] Degrades proteins damaged by L-isoaspartyl residue formation (also known as beta-Asp residues). Degrades L-isoaspartyl-containing di- and maybe also tripeptides. Also has L-asparaginase activity, although this may not be its principal function.<ref>PMID:11988085</ref>  May be involved in glutathione, and possibly other peptide, transport, although these results could also be due to polar effects of disruption.<ref>PMID:11988085</ref>
[[Category: Imiolczyk, B]]
== References ==
[[Category: Bonarek, P]]
<references/>
[[Category: Jaskolski, M]]
__TOC__
[[Category: Kadziolka, K]]
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Barciszewski J]]
[[Category: Bonarek P]]
[[Category: Brzezinski K]]
[[Category: Imiolczyk B]]
[[Category: Jaskolski M]]
[[Category: Kadziolka K]]
[[Category: Klonecka A]]
[[Category: Loch JI]]

Latest revision as of 16:23, 1 February 2024

Structure of E.coli Class 2 L-asparaginase EcAIII, wild type (WT EcAIII)Structure of E.coli Class 2 L-asparaginase EcAIII, wild type (WT EcAIII)

Structural highlights

7qy6 is a 4 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.65Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

IAAA_ECOLI Degrades proteins damaged by L-isoaspartyl residue formation (also known as beta-Asp residues). Degrades L-isoaspartyl-containing di- and maybe also tripeptides. Also has L-asparaginase activity, although this may not be its principal function.[1] May be involved in glutathione, and possibly other peptide, transport, although these results could also be due to polar effects of disruption.[2]

References

  1. Hejazi M, Piotukh K, Mattow J, Deutzmann R, Volkmer-Engert R, Lockau W. Isoaspartyl dipeptidase activity of plant-type asparaginases. Biochem J. 2002 May 15;364(Pt 1):129-36. PMID:11988085
  2. Hejazi M, Piotukh K, Mattow J, Deutzmann R, Volkmer-Engert R, Lockau W. Isoaspartyl dipeptidase activity of plant-type asparaginases. Biochem J. 2002 May 15;364(Pt 1):129-36. PMID:11988085

7qy6, resolution 1.65Å

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