This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1wsa

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:48, 14 February 2024) (edit) (undo)
 
(17 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1wsa.gif|left|200px]]<br />
 
-
<applet load="1wsa" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1wsa, resolution 2.2&Aring;" />
 
-
'''STRUCTURE OF L-ASPARAGINASE II PRECURSOR'''<br />
 
-
==Overview==
+
==STRUCTURE OF L-ASPARAGINASE II PRECURSOR==
-
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.
+
<StructureSection load='1wsa' size='340' side='right'caption='[[1wsa]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 +
== 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>
 +
</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>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/ASPG_WOLSU ASPG_WOLSU]
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ws/1wsa_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</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>
-
==About this Structure==
+
==See Also==
-
1WSA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Wolinella_succinogenes Wolinella succinogenes]. Active as [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] Structure known Active Sites: A and B. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1WSA OCA].
+
*[[Asparaginase 3D structures|Asparaginase 3D structures]]
-
 
+
__TOC__
-
==Reference==
+
</StructureSection>
-
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8898907 8898907]
+
[[Category: Large Structures]]
-
[[Category: Asparaginase]]
+
-
[[Category: Single protein]]
+
[[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]]
+
-
[[Category: signal]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 17:32:42 2007''
+

Current revision

STRUCTURE OF L-ASPARAGINASE II PRECURSOR

PDB ID 1wsa

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1wsa"
Personal tools