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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1wsa]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Wolinella_succinogenes Wolinella succinogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WSA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WSA FirstGlance]. <br>
<table><tr><td colspan='2'>[[1wsa]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Wolinella_succinogenes Wolinella succinogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WSA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WSA FirstGlance]. <br>
</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Asparaginase Asparaginase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.1 3.5.1.1] </span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</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=1wsa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wsa OCA], [https://pdbe.org/1wsa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wsa RCSB], [https://www.ebi.ac.uk/pdbsum/1wsa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wsa 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=1wsa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wsa OCA], [https://pdbe.org/1wsa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wsa RCSB], [https://www.ebi.ac.uk/pdbsum/1wsa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wsa ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ASPG_WOLSU ASPG_WOLSU]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1wsa ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1wsa ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The amino acid sequence and tertiary structure of Wolinella succinogenes L-asparaginase were determined, and were compared with the structures of other type-II bacterial L-asparaginases. Each chain of this homotetrameric enzyme consists of 330 residues. The amino acid sequence is 40-50% identical to the sequences of related proteins from other bacterial sources, and all residues previously shown to be crucial for the catalytic action of these enzymes are identical. Differences between the amino acid sequence of W. succinogenes L-asparaginase and that of related enzymes are discussed in terms of the possible influence on the substrate specificity. The overall fold of the protein subunit is almost identical to that observed for other L-asparaginases. Two fragments in each subunit, a very highly flexible loop (approximately 20 amino acids) that forms part of the active site, and the N-terminus (two amino acids), are not defined in the structure. The orientation of Thr14, a residue probably involved in the catalytic activity, indicates the absence of ligand in the active-site pocket. The rigid part of the active site, which includes the asparaginase triad Thr93-Lys 166-Asp94, is structurally very highly conserved with equivalent regions found in other type-II bacterial L-asparaginases.
Crystal structure and amino acid sequence of Wolinella succinogenes L-asparaginase.,Lubkowski J, Palm GJ, Gilliland GL, Derst C, Rohm KH, Wlodawer A Eur J Biochem. 1996 Oct 1;241(1):201-7. PMID:8898907<ref>PMID:8898907</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1wsa" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Asparaginase 3D structures|Asparaginase 3D structures]]
*[[Asparaginase 3D structures|Asparaginase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Asparaginase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Wolinella succinogenes]]
[[Category: Wolinella succinogenes]]
[[Category: Derst, C]]
[[Category: Derst C]]
[[Category: Gilliland, G L]]
[[Category: Gilliland GL]]
[[Category: Lubkowski, J]]
[[Category: Lubkowski J]]
[[Category: Palm, G J]]
[[Category: Palm GJ]]
[[Category: Rohm, K H]]
[[Category: Rohm K-H]]
[[Category: Wlodawer, A]]
[[Category: Wlodawer A]]
[[Category: Hydrolase]]
[[Category: Periplasmic]]

Latest revision as of 08:48, 14 February 2024

STRUCTURE OF L-ASPARAGINASE II PRECURSOR

1wsa, resolution 2.20Å

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