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2gez

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Revision as of 07:22, 20 June 2018

Crystal structure of potassium-independent plant asparaginase

Structural highlights

2gez is a 8 chain structure with sequence from European yellow lupine. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	1k2x, 1jn9, 1t3m, 1seo, 1apy, 2gaw, 2a8j
Activity:	Asparaginase, with EC number 3.5.1.1
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ASPG_LUPLU] Degrades proteins damaged by L-isoaspartyl residue formation (also known as beta-Asp residues). Also has L-asparaginase activity, which is used to liberate stored nitrogen during seed development.

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

In plants, specialized enzymes are required to catalyze the release of ammonia from asparagine, which is the main nitrogen-relocation molecule in these organisms. In addition, K+-independent plant asparaginases are also active in splitting the aberrant isoaspartyl peptide bonds, which makes these proteins important for seed viability and germination. Here, we present the crystal structure of potassium-independent L-asparaginase from yellow lupine (LlA) and confirm the classification of this group of enzymes in the family of Ntn-hydrolases. The alpha- and beta-subunits that form the mature (alphabeta)2 enzyme arise from autoproteolytic cleavage of two copies of a precursor protein. In common with other Ntn-hydrolases, the (alphabeta) heterodimer has a sandwich-like fold with two beta-sheets flanked by two layers of alpha-helices (alphabetabetaalpha). The nucleophilic Thr193 residue, which is liberated in the autocatalytic event at the N terminus of subunit beta, is part of an active site that is similar to that observed in a homologous bacterial enzyme. An unusual sodium-binding loop of the bacterial protein, necessary for proper positioning of all components of the active site, shows strictly conserved conformation and metal coordination in the plant enzyme. A chloride anion complexed in the LlA structure marks the position of the alpha-carboxylate group of the L-aspartyl substrate/product moiety. Detailed analysis of the active site suggests why the plant enzyme hydrolyzes asparagine and its beta-peptides but is inactive towards substrates accepted by similar Ntn-hydrolases, such as taspase1, an enzyme implicated in some human leukemias. Structural comparisons of LlA and taspase1 provide interesting insights into the role of small inorganic ions in the latter enzyme.

Crystal structure of plant asparaginase.,Michalska K, Bujacz G, Jaskolski M J Mol Biol. 2006 Jun 30;360(1):105-16. Epub 2006 May 15. PMID:16725155^[1]

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

References

↑ Michalska K, Bujacz G, Jaskolski M. Crystal structure of plant asparaginase. J Mol Biol. 2006 Jun 30;360(1):105-16. Epub 2006 May 15. PMID:16725155 doi:10.1016/j.jmb.2006.04.066

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/2gez"

@@ Line 1: / Line 1: @@
 ==Crystal structure of potassium-independent plant asparaginase==
 <StructureSection load='2gez' size='340' side='right' caption='[[2gez]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2gez]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/European_yellow_lupin European yellow lupin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GEZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2GEZ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2gez]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/European_yellow_lupine European yellow lupine]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GEZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2GEZ FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1k2x|1k2x]], [[1jn9|1jn9]], [[1t3m|1t3m]], [[1seo|1seo]], [[1apy|1apy]], [[2gaw|2gaw]], [[2a8j|2a8j]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Asparaginase Asparaginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.1 3.5.1.1] </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=2gez FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gez OCA], [http://pdbe.org/2gez PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2gez RCSB], [http://www.ebi.ac.uk/pdbsum/2gez PDBsum]</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=2gez FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gez OCA], [http://pdbe.org/2gez PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2gez RCSB], [http://www.ebi.ac.uk/pdbsum/2gez PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2gez ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 14: / Line 15: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ge/2gez_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ge/2gez_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 38: / Line 39: @@
 </StructureSection>
 [[Category: Asparaginase]]
-[[Category: European yellow lupin]]
+[[Category: European yellow lupine]]
 [[Category: Bujacz, G]]
 [[Category: Jaskolski, M]]

2gez

From Proteopedia

Revision as of 07:22, 20 June 2018

Crystal structure of potassium-independent plant asparaginase

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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