1esp

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1esp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1esp, resolution 2.8&Aring;" /> '''NEUTRAL PROTEASE MUTA...)
Current revision (07:06, 7 February 2024) (edit) (undo)
 
(16 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1esp.jpg|left|200px]]<br /><applet load="1esp" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1esp, resolution 2.8&Aring;" />
 
-
'''NEUTRAL PROTEASE MUTANT E144S'''<br />
 
-
==Overview==
+
==NEUTRAL PROTEASE MUTANT E144S==
-
The X-ray crystal structure of the Bacillus cereus neutral protease (CNP), active-site mutant E144S, in which the putative general base proposed for, the thermolysin-like zinc neutral proteases, Glu144, has been replaced by, serine, has been determined to a resolution of 2.8 A. This represents the, first crystal structure of an active-site mutant of a zinc neutral, protease. The E 144S mutant was crystallized in the hexagonal space group, P6(5)22, with unit-cell dimensions a = b = 76.57, c = 201.91 A. Although, the ligands involved in zinc coordination in the active site are identical, to those found in the wild-type protein, the mutation results in a, modified environment around the zinc ion; particularly with respect to the, water molecules. While the structure of the mutant is similar to that of, wild type, its protease activity is reduced to 0.16% that of the wild-type, CNP and the protein is virtually resistant to autolysis in the presence of, calcium. The lowered protease activity of the mutant is consistent with, the role proposed for Glu144 as the general base in the catalysis of, thermolysin-like neutral proteases [Matthews (1988). Acc. Chem. Res. 21, 333-340]. We suggest that the residual activity of the E144S mutant arises, from a water molecule, which is found within hydrogen-bonding distance of, Ser144, acting as a general base in the catalytic function of the mutant.
+
<StructureSection load='1esp' size='340' side='right'caption='[[1esp]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
-
 
+
== Structural highlights ==
-
==About this Structure==
+
<table><tr><td colspan='2'>[[1esp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ESP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ESP FirstGlance]. <br>
-
1ESP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus] with CA and ZN as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ESP OCA].
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
-
 
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-
==Reference==
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1esp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1esp OCA], [https://pdbe.org/1esp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1esp RCSB], [https://www.ebi.ac.uk/pdbsum/1esp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1esp ProSAT]</span></td></tr>
-
E144S active-site mutant of the Bacillus cereus thermolysin-like neutral protease at 2.8 A resolution., Lister SA, Wetmore DR, Roche RS, Codding PW, Acta Crystallogr D Biol Crystallogr. 1996 May 1;52(Pt 3):543-50. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15299677 15299677]
+
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/NPRE_BACCE NPRE_BACCE] Extracellular zinc metalloprotease.
 +
== 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/es/1esp_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=1esp ConSurf].
 +
<div style="clear:both"></div>
 +
__TOC__
 +
</StructureSection>
[[Category: Bacillus cereus]]
[[Category: Bacillus cereus]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Codding, P.W.]]
+
[[Category: Codding PW]]
-
[[Category: Litster, S.A.]]
+
[[Category: Litster SA]]
-
[[Category: Roche, R.S.]]
+
[[Category: Roche RS]]
-
[[Category: Wetmore, D.R.]]
+
[[Category: Wetmore DR]]
-
[[Category: CA]]
+
-
[[Category: ZN]]
+
-
[[Category: inactive mutant e144s]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:17:04 2007''
+

Current revision

NEUTRAL PROTEASE MUTANT E144S

PDB ID 1esp

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/1esp"
Personal tools