8bkf: Difference between revisions

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New page: '''Unreleased structure''' The entry 8bkf is ON HOLD Authors: Sciuk, A., Ruszkowski, M., Jaskolski, M., Loch, J.I. Description: Structure of E. coli Class 2 L-asparaginase EcAIII, muta...
 
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'''Unreleased structure'''


The entry 8bkf is ON HOLD
==Structure of E. coli Class 2 L-asparaginase EcAIII, mutant M200T (crystal M200T#o)==
 
<StructureSection load='8bkf' size='340' side='right'caption='[[8bkf]], [[Resolution|resolution]] 1.22&Aring;' scene=''>
Authors: Sciuk, A., Ruszkowski, M., Jaskolski, M., Loch, J.I.
== Structural highlights ==
 
<table><tr><td colspan='2'>[[8bkf]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8BKF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8BKF FirstGlance]. <br>
Description: Structure of E. coli Class 2 L-asparaginase EcAIII, mutant M200T (crystal M200T#1)
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.221&#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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
[[Category: Ruszkowski, M]]
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8bkf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8bkf OCA], [https://pdbe.org/8bkf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8bkf RCSB], [https://www.ebi.ac.uk/pdbsum/8bkf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8bkf ProSAT]</span></td></tr>
[[Category: Loch, J.I]]
</table>
[[Category: Sciuk, A]]
== Function ==
[[Category: Jaskolski, M]]
[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>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Jaskolski M]]
[[Category: Loch JI]]
[[Category: Ruszkowski M]]
[[Category: Sciuk A]]

Latest revision as of 11:18, 7 February 2024

Structure of E. coli Class 2 L-asparaginase EcAIII, mutant M200T (crystal M200T#o)Structure of E. coli Class 2 L-asparaginase EcAIII, mutant M200T (crystal M200T#o)

Structural highlights

8bkf is a 4 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.221Å
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

8bkf, resolution 1.22Å

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